By Professor Dietmar Schomburg, Dr. Ida Schomburg (auth.), Professor Dietmar Schomburg, Dr. Ida Schomburg (eds.)
Springer guide of Enzymes offers information on enzymes sufficiently good characterised. It bargains concise and entire descriptions of a few 5,000 enzymes and their software components. information sheets are prepared of their EC-Number series and the volumes themselves are prepared in accordance with enzyme sessions. This new, moment variation displays substantial growth in enzymology: many enzymes are newly categorised or reclassified. each one access is correlated with references and a number of resource organisms. New datafields are created: software and engineering (for the houses of enzymes the place the series has been changed). the whole quantity of fabric inside the instruction manual has greater than doubled in order that the whole moment variation includes 39 volumes in addition to a Synonym Index. moreover, beginning in 2009, all newly categorised enzymes are taken care of in complement Volumes. Springer instruction manual of Enzymes is a perfect resource of data for researchers in biochemistry, biotechnology, natural and analytical chemistry, and meals sciences, in addition to for medicinal applications.
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Extra resources for Class 1 Oxidoreductases: EC 1
299 Systematic name (S)-malate:NAD(P)+ oxidoreductase Recommended name malate dehydrogenase [NAD(P)+ ] Synonyms MDH II <1> (<1> uses both NADP+ and NAD+ )  CAS registry number 9001-64-3 (cf. )  P l-malate + NADP+ S Additional information <1,2> (<1> no substrate: pyruvate ; <2> enzyme shows pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme. No substrates are: dmalate, malonate, l-glutamate, l-aspartate, dl-2-hydroxybutanoate, dl-3D.
J. Mol. )  P ? )  P d-ribulose 5-phosphate + NADPH + H+ D. Schomburg and I. )  P d-arabitol 1-phosphate + NAD+ S Additional information <1> (<1> participates in arabitol catabolism via the arabitol phosphate route ; <1> no activity with: xylitol 5-phosphate, d-sorbitol, d-mannitol, xylitol, erythrose 4-phosphate and ribose 5-phosphate. )  P ? Inhibitors EDTA <1> (<1> xylulose 5-phosphate does not protect the enzyme from EDTA inactivation. Addition of Mn2+ at concentrations of up to 2 mM results in complete reactivation of APDH )  Hg2+ <1> (<1> 2 mM, complete inactivation )  PHMB <1> (<1> 2 mM, complete inactivation )  Zn2+ <1> (<1> 2 mM, complete inactivation )  Cofactors/prosthetic groups NAD+ <1> (<1> the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH )  NADH <1,2> (<1> the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH ) [1,2] NADP+ <1> (<1> the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH )  NADPH <1> (<1> the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH )  Metals, ions Mn2+ <1> (<1> required.
Gen. 368 kDa retinal reductase in New Zealand white rabbit liver cytosol encoded by the peroxisomal retinol dehydrogenase-reductase cDNA: purification and characterization of the enzyme. Biochem. : Effect of lipid peroxidation products on the activity of human retinol dehydrogenase 12 (RDH12) and retinoid metabolism. Biochim. Biophys. : Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity. : Expression of a novel alternatively spliced variant of NADP(H)-dependent retinol dehydrogenase/reductase with deletion of exon 3 in cervical squamous carcinoma.