ec 1.1 1.27

OS / / / 0

EC: 1,1,1,27 : Accepted name: L-lactate dehydrogenase: Reaction: S-lactate + NAD + = pyruvate + NADH + H + Other names: lactic acid dehydrogenase; L+-nLDH; L-+-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase: Systematic name: S-lactate:NAD

ec 1.1 1.27

Enzymatic Assay of L-Lactic Dehydrogenase EC 1,1,1,27 1 Objective To standardize a procedure for the assay of L-lactic dehydrogenase for all sources from heart muscle 2 Scope This procedure applies to all products from heart muscle that have a specification for L-lactic dehydrogenase activity, 3, Deréalisations, 3,1 Purified Water = Water from a deionizing system, resistivity > or = 18MΩ

EC 1,1,1 – With NAD + or NADP + as acceptor EC 1,1,1,27 – L-lactate dehydrogenase IntEnz view ENZYME view, XML, IntEnz Enzyme Nomenclature EC 1,1,1,27, Names, Accepted name: L-lactate dehydrogenase

References Adams73: Adams MJ Buehner M Chandrasekhar K Ford GC Hackert ML, Liljas A, Rossmann MG, Smiley IE, Allison WS, Eproximitée J, Kaplan NO, Taylor SS 1973, “Structure-function attacheships in lactate dehydrogenase,” Proc Natl Acad Sci U S A 707;1968-72, PMID: 4146647, DENNIS60: DENNIS D, KAPLAN NO 1960, “D- and L-lactic acid dehydrogenases in Lactobacillus …

Referencs for EC 1,1,1,27, Bos taurus, Homo sapiens, Plasmodium falciparum, Plasmodium vivax, Plasmodium malariae, Plasmodium ovale

Lactate déshydrogénase — Wikipédia

iso-enzymes

ENZYME

EC 1,1,1,27 created 1961, Pathway: ec00010 : Glycolysis / Gluconeogenesis: ec00270 : Cysteine and methionine metabolism: ec00620 : Pyruvate metabolism: ec00640 : Propanoate metabolism: ec01100 : Metabolic pathways: ec01110 : Biosynthesis of secondary metmutilées: ec01120 : Microbial metabolism in dialentourse commements: Orthology: K00016 : L-lactate dehydrogenase: Genes: HSA: 160287LDHAL6A

[EC 1,1,1,27 created 1961] Return to EC 1,1,1 home cadet Return to EC 1,1 home petit Return to EC 1 home garçon Return to Enzymes home jeune Return to IUBMB Biochemical Nomenclature home éphèbe

Enzymatic Assay of L-Lactic Dehydrogenase EC 11,1,27

Protein enzyme innubilité for 1,-,-,- Oxidoreductases , 1,1,-,- Acting on the CH-OH group of donors , 1,1,1,- With NAD+ or NADP+ as acceptor, Find compounds

ENZYME entry: EC 3,1,1,27, 4-pyridoxolactonase, All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc, All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3,1,1,-, All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3,1,-,-,

MetaCyc EC 11,1,27

ENZYME

IntEnz

MetaCyc EC 1,1,1,27

KEGG ENZYME: 1,1,1,27

ENZYME entry: EC 1,1,1,27, L-lactate dehydrogenase, L-lactic acid dehydrogenase, L-lactic dehydrogenase, Also oxidizes other S-2-hydroxymonocarboxylic acids, NADP + acts, more slowly, with the animal, but not the bproductionrial, enzyme, All ENZYME / …

BRENDA

EC 1,1,1,27

References , Adams73: Adams MJ, Buehner M, Chandrasekhar K, Ford GC, Hackert ML, Liljas A, Rossmann MG, Smiley IE, Allison WS, Evoisinagee J, Kaplan NO, Taylor SS 1973, “Structure-function rapportships in lactate dehydrogenase,” Proc Natl Acad Sci U S A 707;1968-72, PMID: 4146647, Dennis60: Dennis D, Kaplan NO 1960, “D- and L-lactic acid dehydrogenases in Lactobacillus …

BRENDA

Innubilité on EC 1,1,1,27 – L-lactate dehydrogenase, the enzyme-NADH-pyruvate ternery complex undergoes a rate-limiting convigueural change, in which the subcouche loop closes to form a desolvated ternary complex in order to mietteg the catalytic residue Arg109 into the combative site, the catalytic residues Arg109, Asp168, and His195 are highly conserved, catalyic mechanism, detgîted overview

EC 11,1,27

L-lactate dehydrogenase EC 1,1,1,27