Einar Sørensen

L-erythro-3,5-diaminohexanoate dehydrogenase

dopachrome isomerase

L-arginine:oxygen 2-oxidoreductase (decarboxylating)

L-cut

L-arginine,NAD(P)H:oxygen oxidoreductase (nitric-oxide-forming)

L-arabinose

L-iditol 2-dehydrogenase

In enzymology, a L-ascorbate peroxidase (EC 1.11.1.11) is an enzyme that catalyzes the chemical reactionL-ascorbate + H2O2 ⇌ {\displaystyle \rightleftharpoons } dehydroascorbate + 2 H2OThus, the two substrates of this enzyme are L-ascorbate and H2O2, whereas its two products are dehydroascorbate and H2O.This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is L-ascorbate:hydrogen-peroxide oxidoreductase. Other names in common use include L-ascorbic acid peroxidase, L-ascorbic acid-specific peroxidase, ascorbate peroxidase, and ascorbic acid peroxidase. This enzyme participates in ascorbate and aldarate metabolism.

L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase (EC 6.3.1.13, MshC, MshC ligase, Cys:GlcN-Ins ligase, mycothiol ligase) is an enzyme with systematic name L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming). This enzyme catalyses the following chemical reaction1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP ⇌ {\displaystyle \rightleftharpoons } 1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphateThis enzyme is a key enzyme in the biosynthesis of mycothiol.

L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase

L-infinity-norm

L-indistinguishable

L-group

L-glutamate oxidase

L-event

L-form bacteria, also known as L-phase bacteria, L-phase variants, and cell wall-deficient (CWD) bacteria, are strains of bacteria that lack cell walls. They were first isolated in 1935 by Emmy Klieneberger-Nobel, who named them "L-forms" after the Lister Institute in London where she was working.Two types of L-forms are distinguished: unstable L-forms, spheroplasts that are capable of dividing, but can revert to the original morphology, and stable L-forms, L-forms that are unable to revert to the original bacteria.Some parasitic species of bacteria, such as mycoplasma, also lack a cell wall, but these are not considered L-forms since they are not derived from bacteria that normally have cell walls.

L-aspartate:phenylpyruvate aminotransferase

L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase

L-cysteate sulfo-lyase

L-askorbat:oxygen oxidoreductase

In enzymology, a L-cysteate sulfo-lyase (EC 4.4.1.25) is an enzyme that catalyzes the chemical reactionL-cysteate + H2O ⇌ {\displaystyle \rightleftharpoons } pyruvate + bisulfite + NH3Thus, the two substrates of this enzyme are L-cysteate and H2O, whereas its 3 products are pyruvate, bisulfite, and NH3.This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases.

L-asparagine:tRNAAsn ligase (AMP-forming)

L-galactono-1,4-lactone:oxygen 3-oxidoreductase

In enzymology, a L-idonate 5-dehydrogenase (EC 1.1.1.264) is an enzyme that catalyzes the chemical reactionL-idonate + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } 5-dehydrogluconate + NAD(P)H + H+The 3 substrates of this enzyme are L-idonate, NAD+, and NADP+, whereas its 4 products are 5-dehydrogluconate, NADH, NADPH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.

In enzymology, a L-aspartate oxidase (EC 1.4.3.16) is an enzyme that catalyzes the chemical reactionL-aspartate + H2O + O2 ⇌ {\displaystyle \rightleftharpoons } oxaloacetate + NH3 + H2O2The 3 substrates of this enzyme are L-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, NH3, and H2O2.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-aspartate:oxygen oxidoreductase (deaminating). This enzyme participates in alanine and aspartate metabolism and nicotinate and nicotinamide metabolism. It employs one cofactor, FAD.

L-aspartate:oxygen oxidoreductase

L-aspartate ammonia-lyase (fumarate-forming)

L-cysteine:2-oxoglutarate aminotransferase

L-histidine

L-ascorbic acid 6-hexadecanoate

L-ascorbate peroxidase

L-cysteine:molybdenum cofactor sulfurtransferase

An L-kick is a movement in capoeira, breakdancing and other martial arts and dance forms. It is executed by throwing the body into a cartwheel motion, but rather than completing the wheel, the body flexes while supported by one hand on the ground. One leg is brought downwards and forwards in a kicking motion while the other remains in the air (giving rise to the name).

Fucose_iso_C

In enzymology, a L-idonate 5-dehydrogenase (EC 1.1.1.264) is an enzyme that catalyzes the chemical reactionL-idonate + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } 5-dehydrogluconate + NAD(P)H + H+The 3 substrates of this enzyme are L-idonate, NAD+, and NADP+, whereas its 4 products are 5-dehydrogluconate, NADH, NADPH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-idonate:NAD(P)+ oxidoreductase.

L-citrulline:L-aspartate ligase (AMP-forming)

L-class blimp

L-gulonolactone oxidase (EC 1.1.3.8) is an enzyme that produces vitamin C, but is non-functional in Haplorrhini (including humans), in some bats, and in guinea pigs. It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to L-xylo-hex-3-gulonolactone and hydrogen peroxide. It uses FAD as a cofactor. The L-xylo-hex-3-gulonolactone (2-keto-gulono-gamma-lactone) is able to convert to hexuronic acid (ascorbic acid) spontaneously, without enzymatic action.

L-glutamyl-(BtrI acyl-carrier protein) decarboxylase (EC 4.1.1.95, btrK (gene)) is an enzyme with systematic name L-glutamyl-(BtrI acyl-carrier protein) carboxy-lyase. This enzyme catalyses the following chemical reactionL-glutamyl-[BtrI acyl-carrier protein] ⇌ {\displaystyle \rightleftharpoons } 4-amino butanoyl-[BtrI acyl-carrier protein] + CO2This enzyme binds pyridoxal 5'-phosphate.

L-head

L-attributed grammars are a special type of attribute grammars. They allow the attributes to be evaluated in one depth-first left-to-right traversal of the abstract syntax tree.

* List of airships of the United States Navy

L-glutamate:L-cysteine gamma-ligase (ADP-forming)

L-arabinitol 4-dehydrogenase

L-arabinitol 2-dehydrogenase

In enzymology, a L-arabinokinase (EC 2.7.1.46) is an enzyme that catalyzes the chemical reactionATP + L-arabinose ⇌ {\displaystyle \rightleftharpoons } ADP + beta-L-arabinose 1-phosphateThus, the two substrates of this enzyme are ATP and L-arabinose, whereas its two products are ADP and beta-L-arabinose 1-phosphate.This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-arabinose 1-phosphotransferase. This enzyme is also called L-arabinokinase (phosphorylating). This enzyme participates in nucleotide sugars metabolism.

In enzymology, a L-erythro-3,5-diaminohexanoate dehydrogenase (EC 1.4.1.11) is an enzyme that catalyzes the chemical reactionL-erythro-3,5-diaminohexanoate + H2O + NAD+ ⇌ {\displaystyle \rightleftharpoons } (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+The 3 substrates of this enzyme are L-erythro-3,5-diaminohexanoate, H2O, and NAD+, whereas its 4 products are (S)-5-amino-3-oxohexanoate, NH3, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating). This enzyme is also called L-3,5-diaminohexanoate dehydrogenase. This enzyme participates in lysine degradation.

L-forms

L-class submarine (disambiguation)

L-isoleucine,NADPH:oxygen oxidoreductase

L-gulonolactone oxidase

L-cysteine hydrogen-sulfide-lyase (adding sulfite; L-cysteate-forming)

CL0393

L-arabinonolactonase

L-gulose

L-diversity

L-arginine,2-oxoglutarate:oxygen oxidoreductase

L-galactose 1-dehydrogenase

L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase

Charles Camilleri

L-glutamine(L-asparagine) amidohydrolase

L-cystine

L-glutamine:7-cyano-7-carbaguanine aminotransferase

L-histidinol-phosphate phosphohydrolase

L-glucuronate reductase

L-glutamine:phenylpyruvate aminotransferase

L-erythro-7,8-dihydrobiopterin:NADP+ oxidoreductase

In enzymology, a L-erythro-3,5-diaminohexanoate dehydrogenase (EC 1.4.1.11) is an enzyme that catalyzes the chemical reactionL-erythro-3,5-diaminohexanoate + H2O + NAD+ ⇌ {\displaystyle \rightleftharpoons } (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+The 3 substrates of this enzyme are L-erythro-3,5-diaminohexanoate, H2O, and NAD+, whereas its 4 products are (S)-5-amino-3-oxohexanoate, NH3, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor.

L-carnatine

L-arabinose isomerase

In enzymology, a L-arabinitol 2-dehydrogenase (EC 1.1.1.13) is an enzyme that catalyzes the chemical reactionL-arabinitol + NAD+ ⇌ {\displaystyle \rightleftharpoons } L-ribulose + NADH + H+Thus, the two substrates of this enzyme are L-arabinitol and NAD+, whereas its 3 products are L-ribulose, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.

L-enantiomer

Leader of L-group North Einar Sørensen

L-glycol dehydrogenase

L-idonate:NAD(P)+ oxidoreductase

Two

L-field

L-iduronidase

L-arabinose operon

L-ascorbate—cytochrome-b5 reductase

L-cysteine hydrogen-sulfide-lyase (adding hydrogen cyanide; L-3-cyanoalanine-forming)

L-cysteate

L-isoleucine,NADPH:oxygen oxidoreductase (N-hydroxylating)

L-gulono-gamma-lactone oxidase

L-estimate

L-class submarine

In enzymology, a L-ascorbate peroxidase (EC 1.11.1.11) is an enzyme that catalyzes the chemical reactionL-ascorbate + H2O2 ⇌ {\displaystyle \rightleftharpoons } dehydroascorbate + 2 H2OThus, the two substrates of this enzyme are L-ascorbate and H2O2, whereas its two products are dehydroascorbate and H2O.This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases).

L-glucose

In enzymology, a L-aspartate oxidase (EC 1.4.3.16) is an enzyme that catalyzes the chemical reactionL-aspartate + H2O + O2 ⇌ {\displaystyle \rightleftharpoons } oxaloacetate + NH3 + H2O2The 3 substrates of this enzyme are L-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, NH3, and H2O2.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor.

L-cysteine:acceptor sulfurtransferase

L-cxr

L-glutamine:D-fructose-6-phosphate isomerase (deaminating)

L-idonate 5-dehydrogenase

L-glutamate:NAD(P)+ oxidoreductase (deaminating)

Singing This Song

L-histidine:beta-alanine ligase (ADP-forming)

L-arginine carboxy-lyase (agmatine-forming)

L-histidine:2-oxoglutarate aminotransferase

L-arginine

In mathematics, ℓ∞ and L ∞ {\displaystyle L_{\infty }} are two related vector spaces.

L-glutamate:NADP+ oxidoreductase (deaminating)

L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming)

L-caron

L-glutamine:tRNAGln ligase (AMP-forming)

l-diversity is a form of group based anonymization that is used to preserve privacy in data sets by reducing the granularity of a data representation. This reduction is a trade off that results in some loss of effectiveness of data management or mining algorithms in order to gain some privacy. The l-diversity model is an extension of the k-anonymity model which reduces the granularity of data representation using techniques including generalization and suppression such that any given record maps onto at least k other records in the data. The l-diversity model handles some of the weaknesses in the k-anonymity model where protected identities to the level of k-individuals is not equivalent to protecting the corresponding sensitive values that were generalized or suppressed, especially when the sensitive values within a group exhibit homogeneity. The l-diversity model adds the promotion of intra-group diversity for sensitive values in the anonymization mechanism.

L-class destroyer

L-atv

L-gulonate 3-dehydrogenase

L-arginine:glycine amidinotransferase

L-aspartate:L-glutamine amido-ligase (AMP-forming)

L-ascorbate-cytochrome-b5 reductase

L-glutamate:tRNAGlu ligase (AMP-forming)

L-ascorbate oxidase

L-arabinose 1-dehydrogenase

L-cyclic order

L-cysteate bisulfite-lyase (deaminating; pyruvate-forming)

L-arabinokinase

L-glutamate:ammonia ligase (ADP-forming)

L-arabinonate dehydratase

L-aspartate:2-oxoglutarate aminotransferase

L-bar lift

L-aspartate:ammonia ligase (AMP-forming)

L-galactose 1-dehydrogenase (EC 1.1.1.316, L-GalDH, L-galactose dehydrogenase) is an enzyme with systematic name L-galactose:NAD+ 1-oxidoreductase. This enzyme catalyses the following chemical reactionL-galactose + NAD+ ⇌ {\displaystyle \rightleftharpoons } L-galactono-1,4-lactone + NADH + H+The enzyme catalyses a step in the ascorbate biosynthesis in higher plants.

L-citrulline N5-carbamoyldihydrolase

L-aspartate:tRNAAsp ligase (AMP-forming)

In enzymology, a L-dopachrome isomerase (EC 5.3.3.12) is an enzyme that catalyzes the chemical reactionL-dopachrome ⇌ {\displaystyle \rightleftharpoons } 5,6-dihydroxyindole-2-carboxylateHence, this enzyme has one substrate, L-dopachrome, and one product, 5,6-dihydroxyindole-2-carboxylate.This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds.

L-glutamate-semialdehyde:NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming)

L-galactose:NAD+ 1-oxidoreductase

L-hyoscyamine

L-capture

L-breaking

In enzymology, a L-gulonate 3-dehydrogenase (EC 1.1.1.45) is an enzyme that catalyzes the chemical reactionL-gulonate + NAD+ ⇌ {\displaystyle \rightleftharpoons } 3-dehydro-L-gulonate + NADH + H+Thus, the two substrates of this enzyme are L-gulonate and NAD+, whereas its 3 products are 3-dehydro-L-gulonate, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.

L-cysteine:tRNACys ligase (AMP-forming)

L-electron capture

In enzymology, a L-galactonolactone oxidase (EC 1.3.3.12) is an enzyme that catalyzes the chemical reactionL-galactono-1,4-lactone + O2 ⇌ {\displaystyle \rightleftharpoons } L-ascorbate + H2O2Thus, the two substrates of this enzyme are L-galactono-1,4-lactone and O2, whereas its two products are L-ascorbic acid and H2O2.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-galactono-1,4-lactone:oxygen 3-oxidoreductase. This enzyme is also called L-galactono-1,4-lactone oxidase. This enzyme participates in ascorbic acid and aldaric acid metabolism. It employs one cofactor, FAD.

L-iduronate-2-sulfate 2-sulfohydrolase

L-histidine carboxy-lyase (histamine-forming)

L-arginine,NADPH:oxygen oxidoreductase (nitric-oxide-forming)

L-arabinose aldose-ketose-isomerase

L-glutamate:coenzyme F420-1 ligase

L-arginine aminopeptidase

L-fucose isomerase, second N-terminal domain

In enzymology, a L-fuculose-phosphate aldolase (EC 4.1.2.17) is an enzyme that catalyzes the chemical reactionL-fuculose-1-phosphate ⇌ {\displaystyle \rightleftharpoons } glycerone phosphate + (S)-lactaldehydeHence, this enzyme has one substrate, L-fuculose-1-phosphate, and two products, glycerone phosphate and (S)-lactaldehyde.This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds.

In enzymology, a L-glycol dehydrogenase (EC 1.1.1.185) is an enzyme that catalyzes the chemical reactionan L-glycol + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } a 2-hydroxycarbonyl compound + NAD(P)H + H+The 3 substrates of this enzyme are L-glycol, NAD+, and NADP+, whereas its 4 products are 2-hydroxycarbonyl compound, NADH, NADPH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glycol:NAD(P)+ oxidoreductase. Other names in common use include glycol (nicotinamide adenine dinucleotide (phosphate)), dehydrogenase, L-(+)-glycol:NAD(P)+ oxidoreductase, and L-glycol:NAD(P)+ dehydrogenase.

L-carnosine

L-glutamate:putrescine ligase (ADP-forming)

l-diversity is a form of group based anonymization that is used to preserve privacy in data sets by reducing the granularity of a data representation. This reduction is a trade off that results in some loss of effectiveness of data management or mining algorithms in order to gain some privacy.

L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing)

L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)

The L class blimps were training airships operated by the United States Navy during World War II. In the mid-1930s, the Goodyear Aircraft Company built a family of small non-rigid airships that the company used for advertising the Goodyear name. In 1937 the United States Navy awarded a contract for two different airships, K class blimp designated K-2 and a smaller blimp based upon Goodyear’s smaller commercial model airship used for advertising and passenger carrying.

L-glutamate:coenzyme gamma-F420-2 (ADP-forming)

An L-kick is a movement in capoeira, breakdancing and other martial arts and dance forms. It is executed by throwing the body into a cartwheel motion, but rather than completing the wheel, the body flexes while supported by one hand on the ground. One leg is brought downwards and forwards in a kicking motion while the other remains in the air (giving rise to the name). The kick is sometimes held, like a freeze, then returned to standing.Variations include a shotgun kick, in which the non-kicking leg is bent dramatically towards the body so that the legs resemble a shotgun shape, an elbow L-kick where the kick is supported by the elbow and forearm placed on the ground rather than just a hand, and a capoeira switch where L-kicks are performed with first one leg then the other, in different directions and without landing the cartwheel motion.The move was introduced to the b-boy world by Chris Gatdula aka Cristyle of the acclaimed dance group Jabbawockeez.

The L-arabinose operon, also called the ara or araBAD operon, is an operon that encodes enzymes needed for the catabolism of arabinose in Escherichia coli. It has both positive and negative regulation and is activated allosterically.It has been a focus for research in molecular biology since 1970, and has been investigated extensively at its genetic, biochemical, physiological, and biophysical levels.In E. coli, arabinose is converted to xylulose 5-phosphate, an intermediate of the pentose phosphate pathway.

L-fructose

In enzymology, a L-arabinonate dehydratase (EC 4.2.1.25) is an enzyme that catalyzes the chemical reactionL-arabinonate ⇌ {\displaystyle \rightleftharpoons } 2-dehydro-3-deoxy-L-arabinonate + H2OHence, this enzyme has one substrate, L-arabinonate, and two products, 2-dehydro-3-deoxy-L-arabinonate and H2O.This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-arabinonate hydro-lyase (2-dehydro-3-deoxy-L-arabinonate-forming). Other names in common use include L-arabonate dehydrase, L-arabonate dehydratase, and L-arabinonate hydro-lyase. This enzyme participates in ascorbate and aldarate metabolism.

L-glutamyl-(BtrI acyl-carrier protein) decarboxylase

The L-groups (Danish: L-gruppe) was a resistance group tasked with assassination of Danish collaborators and German forces occupying Denmark during the Second World War. The precursor to the group was established in 1940, but it was most active from 1944 to the end of the war. The group carried out at least 18 assassination operations and killed between 20 and 30 people. In 1945 the group was hard hit by arrests and killings of its members and further suffered a very high death-rate in the years immediately after the war with suicides and accidents killing a number of members. The group had strong ties to the Danish police, with 5 of its members being police officers.

L-arginine:tRNAArg ligase (AMP-forming)

L-glutamine:pyruvate aminotransferase

L-homoserine

Arabinose isomerase

L-glutamate 2,3-aminomutase

L-arogenate:NAD(P)+ oxidoreductase (decarboxylating)

L-arogenate:NADP+ oxidoreductase (decarboxylating)

L-chiro-inositol

Albert Cassola

L-citrulline

L-glutaminyl-peptide gamma-glutamyltransferase (cyclizing)

In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction2 L-ascorbate + O2 ⇌ {\displaystyle \rightleftharpoons } 2 dehydroascorbate + 2 H2OThus, the two substrates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O.

L-cysteine:NAD+ oxidoreductase

L-homomorphism

(L)-chiro-Inositol

L-cycloserine

L-dihydroxyphenylalanine

L-form bacteria, also known as L-phase bacteria, L-phase variants, and cell wall-deficient (CWD) bacteria, are strains of bacteria that lack cell walls.

L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating)

L-glutamate:NAD+ oxidoreductase (transaminating)

L-drive

l-fucose isomerase from escherichia coli

In enzymology, a L-gulonate 3-dehydrogenase (EC 1.1.1.45) is an enzyme that catalyzes the chemical reactionL-gulonate + NAD+ ⇌ {\displaystyle \rightleftharpoons } 3-dehydro-L-gulonate + NADH + H+Thus, the two substrates of this enzyme are L-gulonate and NAD+, whereas its 3 products are 3-dehydro-L-gulonate, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-gulonate:NAD+ 3-oxidoreductase. Other names in common use include L-3-aldonate dehydrogenase, L-3-aldonic dehydrogenase, L-gulonic acid dehydrogenase, L-beta-hydroxyacid dehydrogenase, L-beta-hydroxy-acid-NAD+-oxidoreductase, and L-3-hydroxyacid dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.

In enzymology, a L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes the chemical reactionL-glutamate + O2 + H2O ⇌ {\displaystyle \rightleftharpoons } 2-oxoglutarate + NH3 + H2O2The 3 substrates of this enzyme are L-glutamate, O2, and H2O, whereas its 3 products are 2-oxoglutarate, NH3, and H2O2.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor.

L-fucose isomerase, first N-terminal domain

L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase

In enzymology, a L-arabinitol 2-dehydrogenase (EC 1.1.1.13) is an enzyme that catalyzes the chemical reactionL-arabinitol + NAD+ ⇌ {\displaystyle \rightleftharpoons } L-ribulose + NADH + H+Thus, the two substrates of this enzyme are L-arabinitol and NAD+, whereas its 3 products are L-ribulose, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arabinitol:NAD+ 2-oxidoreductase (L-ribulose-forming). Other names in common use include L-arabinitol dehydrogenase (ribulose-forming), and L-arabinitol (ribulose-forming) dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.

In enzymology, a L-arabinose 1-dehydrogenase (EC 1.1.1.46) is an enzyme that catalyzes the chemical reactionL-arabinose + NAD+ ⇌ {\displaystyle \rightleftharpoons } L-arabinono-1,4-lactone + NADH + H+Thus, the two substrates of this enzyme are L-arabinose and NAD+, whereas its 3 products are L-arabinono-1,4-lactone, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arabinose:NAD+ 1-oxidoreductase. This enzyme participates in ascorbate and aldarate metabolism.

L-cysteine hydrochloride monohydrate

North, South, Central

L-chiro-Inositol

L-glutamate:histamine ligase

L-homoserine:NAD(P)+ oxidoreductase

Sorbitol dehydrogenase tetramer, Human

L-ghana

L-groups

The L-arabinose operon, also called the ara or araBAD operon, is an operon that encodes enzymes needed for the catabolism of arabinose in Escherichia coli. It has both positive and negative regulation and is activated allosterically.It has been a focus for research in molecular biology since 1970, and has been investigated extensively at its genetic, biochemical, physiological, and biophysical levels.In E.

Osla for n
(WAP345)

Henrik Wessel Platou

In enzymology, a L-cysteate sulfo-lyase (EC 4.4.1.25) is an enzyme that catalyzes the chemical reactionL-cysteate + H2O ⇌ {\displaystyle \rightleftharpoons } pyruvate + bisulfite + NH3Thus, the two substrates of this enzyme are L-cysteate and H2O, whereas its 3 products are pyruvate, bisulfite, and NH3.This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cysteate bisulfite-lyase (deaminating; pyruvate-forming). Other names in common use include L-cysteate sulfo-lyase (deaminating), and CuyA.

L-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming)

L-glutamate:methylamine ligase (ADP-forming)

L-arabinose:NAD+ 1-oxidoreductase

In enzymology, a L-galactonolactone oxidase (EC 1.3.3.12) is an enzyme that catalyzes the chemical reactionL-galactono-1,4-lactone + O2 ⇌ {\displaystyle \rightleftharpoons } L-ascorbate + H2O2Thus, the two substrates of this enzyme are L-galactono-1,4-lactone and O2, whereas its two products are L-ascorbic acid and H2O2.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor.

L-galactose

L-carnitinamide amidohydrolase

L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating)

L-carnitine hydro-lyase (4-(trimethylammonio)but-2-enoate-forming)

L-function with Grössencharakter

L-arginine:pyruvate aminotransferase

L-isoleucine:tRNAIle ligase (AMP-forming)

L-dopachrome isomerase

L-calculus

L-glutamine amidohydrolase

L-cysteine

L-arginine,NAD(P)H:oxygen oxidoreductase

L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)

L-camphor

In enzymology, a L-fucose isomerase (EC 5.3.1.25) is an enzyme that catalyzes the chemical reactionL-fucose ⇌ {\displaystyle \rightleftharpoons } L-fuculoseHence, this enzyme has one substrate, L-fucose, and one product, L-fuculose.This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-fucose aldose-ketose-isomerase.

L-carveol

L-aspartate oxidase

L-deoxyribose

L-glyceraldehyde

In enzymology, a L-fucose isomerase (EC 5.3.1.25) is an enzyme that catalyzes the chemical reactionL-fucose ⇌ {\displaystyle \rightleftharpoons } L-fuculoseHence, this enzyme has one substrate, L-fucose, and one product, L-fuculose.This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-fucose aldose-ketose-isomerase. This enzyme participates in fructose and mannose metabolism.The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases. The structure was determined by X-ray crystallography at 2.5 Angstrom resolution. Each subunit of the hexameric enzyme is wedge-shaped and composed of three domains. Both domains 1 and 2 contain central parallel beta- sheets with surrounding alpha helices. The active centre is shared between pairs of subunits related along the molecular three-fold axis, with domains 2 and 3 from one subunit providing most of the substrate-contacting residues.

L-asparagine amidohydrolase

L-glutamate:coenzyme F420-1 ligase (GDP-forming)

L-glutamate:ferredoxin oxidoreductase (transaminating)

L-class blimps

L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming)

Fucose_iso_N1

L-arginine hydrochloride

In enzymology, a L-dopachrome isomerase (EC 5.3.3.12) is an enzyme that catalyzes the chemical reactionL-dopachrome ⇌ {\displaystyle \rightleftharpoons } 5,6-dihydroxyindole-2-carboxylateHence, this enzyme has one substrate, L-dopachrome, and one product, 5,6-dihydroxyindole-2-carboxylate.This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is L-dopachrome keto-enol isomerase. Other names in common use include dopachrome tautomerase, tyrosinase-related protein 2, TRP-1, TRP2, TRP-2, tyrosinase-related protein-2, dopachrome Delta7,Delta2-isomerase, dopachrome Delta-isomerase, dopachrome conversion factor, dopachrome isomerase, dopachrome oxidoreductase, dopachrome-rearranging enzyme, DCF, DCT, dopachrome keto-enol isomerase, and L-dopachrome-methyl ester tautomerase. This enzyme participates in tyrosine metabolism and melanogenesis.

Arabinose_Isome

L-infinity norm

L-hyoscyamine,2-oxoglutarate:oxygen oxidoreductase ((6S)-hydroxylating)

tac Lacora

L-gulono-1,4-lactone:oxygen 3-oxidoreductase

In enzymology, a L-glycol dehydrogenase (EC 1.1.1.185) is an enzyme that catalyzes the chemical reactionan L-glycol + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } a 2-hydroxycarbonyl compound + NAD(P)H + H+The 3 substrates of this enzyme are L-glycol, NAD+, and NADP+, whereas its 4 products are 2-hydroxycarbonyl compound, NADH, NADPH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.

L-asparagine hydro-lyase (3-cyanoalanine-forming)

L-aspartate:L-glutamine amido-ligase

L-cube

L-arogenate:NAD+ oxidoreductase (decarboxylating)

L-glutamate:tRNAGlx ligase (AMP-forming)

L-form bacteria

L-arginine ethyl ester

In enzymology, a L-arabinose isomerase (EC 5.3.1.4) is an enzyme that catalyzes the chemical reactionL-arabinose ⇌ {\displaystyle \rightleftharpoons } L-ribuloseHence, this enzyme has one substrate, L-arabinose, and one product, L-ribulose.This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase.

Sean Booth and Rob Brown

L-arginine amidinohydrolase

The L class blimps were training airships operated by the United States Navy during World War II. In the mid-1930s, the Goodyear Aircraft Company built a family of small non-rigid airships that the company used for advertising the Goodyear name. In 1937 the United States Navy awarded a contract for two different airships, K class blimp designated K-2 and a smaller blimp based upon Goodyear’s smaller commercial model airship used for advertising and passenger carrying. The smaller blimp was designated by the Navy as L-1 The L-1 was delivered in April 1938 and operated from the Navy’s lighter-than-air facility at Lakehurst, New Jersey. In the meantime, the Navy ordered two more L-Class blimps, the L-2 and L-3, on September 25, 1940. These were delivered in 1941. L-2 was lost in a nighttime mid-air collision with the G-1 on June 8, 1942.When the United States entered World War II, the Navy took over the operation of Goodyear’s five commercial blimps. These were the Resolute, Enterprise, Reliance, Rainbow, and Ranger. These airships were given the designations L-4 through L-8 even though their characteristics and performance varied among them. The next four L-Class airships were built in the assembly and repair shops at NAS Moffett Field. These blimps, L-9 through L-12 were completed by April 1943. The last lot of L-Class airships were ordered from Goodyear under a contract of February 24, 1943. This was a lot of ten airships designated L-13 through L-22. All the blimps were delivered by the end of 1943.As training airships these blimps operated mainly from the two major lighter-than-air bases, Lakehurst and Moffett Field. While too small for any extensive operational use, they were used on some coastal patrols. In this role, L-8, of Blimp Squadron ZP-32 was involved in a mysterious incident where in the airship came drifting in from the Pacific Ocean over southern San Francisco at Daly City on August 16, 1942, without either of the crewmen – Lt. E. D. Cody and Ensign C. Adams – on board. No trace of either man was ever found.Following the end of World War II a number of the L-class blimps were sold back to Goodyear.

L-imħabba

crystal structure of l-arabinose isomerase from e.coli

L-function of an elliptic curve

L-chiro-Inositol is one of the isomers of inositol.

An L-drive is a type of azimuth thruster in which the pod-mounted propellers are driven mechanically rather than electrically. Azimuth thruster pods can be rotated through a full 360 degrees, allowing for rapid changes in thrust direction and eliminating the need for a conventional rudder. This form of power transmission is called a L-drive because the rotary motion has to make one right angle turn, thus looking a bit like the letter "L".

L-form

L-histidinol-phosphate:2-oxoglutarate aminotransferase

L-gulono-1,4-lactone:NADP+ 1-oxidoreductase

L-dopa

L-indistinguishability

L-iditol

L-carnitine

L-fucose aldose-ketose-isomerase

Training airship

L-aspartate:tRNAAsx ligase (AMP-forming)

L-aspartate 4-carboxy-lyase (L-alanine-forming)

L-fenfluramine

L-arogenate:2-oxoglutarate aminotransferase

L-form strains

Malta

L-functions

In enzymology, a L-arabinokinase (EC 2.7.1.46) is an enzyme that catalyzes the chemical reactionATP + L-arabinose ⇌ {\displaystyle \rightleftharpoons } ADP + beta-L-arabinose 1-phosphateThus, the two substrates of this enzyme are ATP and L-arabinose, whereas its two products are ADP and beta-L-arabinose 1-phosphate.This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor.

L-galactonolactone oxidase

L-dopachrome keto-enol isomerase

"L-imħabba"

L-histidine ammonia-lyase (urocanate-forming)

In enzymology, a L-arabinonolactonase (EC 3.1.1.15) is an enzyme that catalyzes the chemical reactionL-arabinono-1,4-lactone + H2O ⇌ {\displaystyle \rightleftharpoons } L-arabinonateThus, the two substrates of this enzyme are L-arabinono-1,4-lactone and H2O, whereas its product is L-arabinonate.This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is L-arabinono-1,4-lactone lactonohydrolase. This enzyme participates in ascorbate and aldarate metabolism.

L-genus

L-ascorbate

Helen Micallef, Joseph Cutajar

L-iduronic acid

L-glycol:NAD(P)+ oxidoreductase

L-aspartate

Marija l-Maltija

eng

L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming)

L-gruppe

L-balance

In enzymology, a L-arabinonate dehydratase (EC 4.2.1.25) is an enzyme that catalyzes the chemical reactionL-arabinonate ⇌ {\displaystyle \rightleftharpoons } 2-dehydro-3-deoxy-L-arabinonate + H2OHence, this enzyme has one substrate, L-arabinonate, and two products, 2-dehydro-3-deoxy-L-arabinonate and H2O.This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds.

L-balance theorem

Maltese

L-group (disambiguation)

L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming)

L-arginine iminohydrolase

M39 Diffain

L-fucose isomerase, C-terminal domain

L-glutamate:coenzyme F420-0 ligase

L-glutamate:oxygen oxidoreductase (deaminating)

In enzymology, a L-arabinitol 4-dehydrogenase (EC 1.1.1.12) is an enzyme that catalyzes the chemical reactionL-arabinitol + NAD+ ⇌ {\displaystyle \rightleftharpoons } L-xylulose + NADH + H+Thus, the two substrates of this enzyme are L-arabinitol and NAD+, whereas its 3 products are L-xylulose, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.

L-histidine decarboxylase

L-carrier

L-gaim

L-kynurenine

L-iditol:NAD+ 2-oxidoreductase

L-event is an EP by electronic music duo Autechre, released on Warp Records on 28 October 2013.

L-class destroyer (disambiguation)

L-aspartate aminopeptidase

L-fucitol

L-fuculokinase

L-fuconate dehydratase

Exai
newbound

L-aspartate 1-carboxy-lyase (beta-alanine-forming)

L-fucose isomerase

In enzymology, a L-arabinonolactonase (EC 3.1.1.15) is an enzyme that catalyzes the chemical reactionL-arabinono-1,4-lactone + H2O ⇌ {\displaystyle \rightleftharpoons } L-arabinonateThus, the two substrates of this enzyme are L-arabinono-1,4-lactone and H2O, whereas its product is L-arabinonate.This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds.

In enzymology, a L-iditol 2-dehydrogenase (EC 1.1.1.14) is an enzyme that catalyzes the chemical reactionL-iditol + NAD+ ⇌ L-sorbose + NADH + H+Thus, the two substrates of this enzyme are L-iditol and NAD+, whereas its 3 products are L-sorbose, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-iditol:NAD+ 2-oxidoreductase.

In enzymology, a L-fuculose-phosphate aldolase (EC 4.1.2.17) is an enzyme that catalyzes the chemical reactionL-fuculose-1-phosphate ⇌ {\displaystyle \rightleftharpoons } glycerone phosphate + (S)-lactaldehydeHence, this enzyme has one substrate, L-fuculose-1-phosphate, and two products, glycerone phosphate and (S)-lactaldehyde.This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming). Other names in common use include L-fuculose 1-phosphate aldolase, fuculose aldolase, and L-fuculose-1-phosphate lactaldehyde-lyase. This enzyme participates in fructose and mannose metabolism.

An L-drive is a type of azimuth thruster in which the pod-mounted propellers are driven mechanically rather than electrically. Azimuth thruster pods can be rotated through a full 360 degrees, allowing for rapid changes in thrust direction and eliminating the need for a conventional rudder. This form of power transmission is called a L-drive because the rotary motion has to make one right angle turn, thus looking a bit like the letter "L". This name is used to make clear the arrangement of drive is different from Z-drive.The Voith-Schneider marine propulsion system (also mechanically linked) can also quickly change the direction of thrust.

changed

L-glutamate:NAD+ oxidoreductase (deaminating)

L-attributed grammars are a special type of attribute grammars. They allow the attributes to be evaluated in one depth-first left-to-right traversal of the abstract syntax tree. As a result, attribute evaluation in L-attributed grammars can be incorporated conveniently in top-down parsing.A syntax-directed definition is L-attributed if each inherited attribute of Xj on the right side ofA → X1 X2 … Xndepends only on1.the attributes of the symbols X1, X2, …, Xj-12.the inherited attributes of AEvery S-attributed syntax-directed definition is also L-attributed.Implementing L-attributed definitions in Bottom-Up parsers requires rewriting L-attributed definitions into translation schemes.Many programming languages are L-attributed. Special types of compilers, the narrow compilers, are based on some form of L-attributed grammar. These are a strict superset of S-attributed grammars. Used for code synthesis.Either ″Inherited attributes″ or ″synthesized attributes″ associated with the occurrence of symbol X1,X2-----Xn

L-fuculose-phosphate aldolase

L-glutamate:coenzyme F420-0 ligase (GDP-forming)

L-arabinono-1,4-lactone lactonohydrolase

L-glutamine:D-alanine gamma-glutamyltransferase

L-cysteine hydrochloride

L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)

L-fuculose

In enzymology, a L-arabinose isomerase (EC 5.3.1.4) is an enzyme that catalyzes the chemical reactionL-arabinose ⇌ {\displaystyle \rightleftharpoons } L-ribuloseHence, this enzyme has one substrate, L-arabinose, and one product, L-ribulose.This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase. This enzyme participates in pentose and glucuronate interconversions.This enzyme catalyses the conversion of L-arabinose to L-ribulose as the first step in the pathway of L-arabinose utilization as a carbon source.

L-glutamic acid decarboxylase

L-glycine

In enzymology, a L-arabinitol 4-dehydrogenase (EC 1.1.1.12) is an enzyme that catalyzes the chemical reactionL-arabinitol + NAD+ ⇌ {\displaystyle \rightleftharpoons } L-xylulose + NADH + H+Thus, the two substrates of this enzyme are L-arabinitol and NAD+, whereas its 3 products are L-xylulose, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming). Other names in common use include pentitol-DPN dehydrogenase, and L-arabitol dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.

L-arginase

Autechre

L-imhabba

L-gulonate:NADP+ 6-oxidoreductase

L-aspartate:NAD(P)+ oxidoreductase (deaminating)

L-asparagine

L-deprenyl

L-epicatechol

L-arabinonate hydro-lyase (2-dehydro-3-deoxy-L-arabinonate-forming)

L-infinity

In enzymology, a L-iditol 2-dehydrogenase (EC 1.1.1.14) is an enzyme that catalyzes the chemical reactionL-iditol + NAD+ ⇌ L-sorbose + NADH + H+Thus, the two substrates of this enzyme are L-iditol and NAD+, whereas its 3 products are L-sorbose, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-iditol:NAD+ 2-oxidoreductase. Other names in common use include polyol dehydrogenase, sorbitol dehydrogenase, L-iditol:NAD+ 5-oxidoreductase, L-iditol (sorbitol) dehydrogenase, glucitol dehydrogenase, L-iditol:NAD+ oxidoreductase, NAD+-dependent sorbitol dehydrogenase, NAD+-dependent sorbitol dehydrogenase, and NAD+-sorbitol dehydrogenase. This enzyme participates in fructose and mannose metabolism.

In enzymology, a L-fuconate dehydratase (EC 4.2.1.68) is an enzyme that catalyzes the chemical reactionL-fuconate ⇌ {\displaystyle \rightleftharpoons } 2-dehydro-3-deoxy-L-fuconate + H2OHence, this enzyme has one substrate, L-fuconate, and two products, 2-dehydro-3-deoxy-L-fuconate and H2O.This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds.

L-cysteine:tRNA sulfurtransferase

L-histidinol:NAD+ oxidoreductase

L-isoleucine

L-homocysteine hydrogen-sulfide-lyase (deaminating; 2-oxobutanoate-forming)

L-askorbat:hydrogen-peroxide oxidoreductase

Warner R-500-2 radials,

L-chain

The L-groups (Danish: L-gruppe) was a resistance group tasked with assassination of Danish collaborators and German forces occupying Denmark during the Second World War. The precursor to the group was established in 1940, but it was most active from 1944 to the end of the war. The group carried out at least 18 assassination operations and killed between 20 and 30 people.

L-glutamate:coenzyme gamma-F420-2

L-glutamate 1-carboxy-lyase (4-aminobutanoate-forming)

L-glutamate

L-infinity-space

L-asparaginase

L-glutamate:ethylamine ligase (ADP-forming)

In enzymology, a L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes the chemical reactionL-glutamate + O2 + H2O ⇌ {\displaystyle \rightleftharpoons } 2-oxoglutarate + NH3 + H2O2The 3 substrates of this enzyme are L-glutamate, O2, and H2O, whereas its 3 products are 2-oxoglutarate, NH3, and H2O2.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-glutamate:oxygen oxidoreductase (deaminating). Other names in common use include glutamate (acceptor) dehydrogenase, glutamate oxidase, glutamic acid oxidase, glutamic dehydrogenase (acceptor), and L-glutamic acid oxidase. It employs one cofactor, FAD.

Fucose_iso_N2

L-dropping

L-infty-Norm

L-ascorbic acid

L-histidine:tRNAHis ligase (AMP-forming)

L-arginyl-tRNA:protein arginyltransferase

L-aspartate:ammonia ligase (ADP-forming)

L-infty-space

L-glutamyl- decarboxylase

L-band

L-asparagine:hydroxylamine gamma-aspartyltransferase

L-infty-norm

L-ascorbate--cytochrome-b5 reductase

L-cysteine:oxygen oxidoreductase

L-head engine

L-askorbat:ferricytochrome-b5 oxidoreductase

L-kick

L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming)

L-glutamine:2,4,63,5-pentahydroxycyclohexanone aminotransferase

L-gulonate:NAD+ 3-oxidoreductase

In enzymology, a L-arabinose 1-dehydrogenase (EC 1.1.1.46) is an enzyme that catalyzes the chemical reactionL-arabinose + NAD+ ⇌ {\displaystyle \rightleftharpoons } L-arabinono-1,4-lactone + NADH + H+Thus, the two substrates of this enzyme are L-arabinose and NAD+, whereas its 3 products are L-arabinono-1,4-lactone, NADH, and H+.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.

L-glutamate:NADP+ oxidoreductase (transaminating)

AE_LIVE

L-arogenate:oxaloacetate aminotransferase

L-class

L-desoxyephedrine

L-fuconate hydro-lyase (2-dehydro-3-deoxy-L-fuconate-forming)

L-asparagine:2-oxo-acid aminotransferase

L-glutamyl-(BtrI acyl-carrier protein) carboxy-lyase

L-erythro-3-hydroxy-aspartate glyoxylate-lyase (glycine-forming)

L-aspartate-4-semialdehyde hydro-lyase

L-attributed grammar

L-arabinosidase

In enzymology, a L-fuconate dehydratase (EC 4.2.1.68) is an enzyme that catalyzes the chemical reactionL-fuconate ⇌ {\displaystyle \rightleftharpoons } 2-dehydro-3-deoxy-L-fuconate + H2OHence, this enzyme has one substrate, L-fuconate, and two products, 2-dehydro-3-deoxy-L-fuconate and H2O.This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-fuconate hydro-lyase (2-dehydro-3-deoxy-L-fuconate-forming). This enzyme is also called L-fuconate hydro-lyase.

L-arginine:1-amino-1-deoxy-scyllo-inositol-4-phosphate amidinotransferase

L-arabinitol:NAD+ 2-oxidoreductase (L-ribulose-forming)

L-cystathionine L-homocysteine-lyase (deaminating; pyruvate-forming)

Helen & Joseph

L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase (EC 6.3.1.13, MshC, MshC ligase, Cys:GlcN-Ins ligase, mycothiol ligase) is an enzyme with systematic name L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming).

L-idonate 2-dehydrogenase

L-glutamine

L-infty-Space

German Occupying Forces

L-bar

L-fucose