By Professor Dr. Dietmar Schomburg, Dr. Dörte Stephan (auth.), Professor Dr. Dietmar Schomburg, Dr. Dörte Stephan (eds.)
Recent development on enzyme immobilisation, enzyme creation, coenzyme re iteration and enzyme engineering has spread out interesting new fields for the aptitude program of enzymes in a wide range of other components. As extra growth in study and alertness of enzymes has been made the inability of an up to date review of enzyme molecular homes has develop into extra appar ent. as a result, we all started the improvement of an enzyme information info sys tem as a part of protein-design actions at GBF. the current publication "Enzyme Hand publication" represents the broadcast model of this information financial institution. In destiny a working laptop or computer searchable model can be additionally to be had. The enzymes during this instruction manual are prepared in keeping with the Enzyme Com challenge record of enzymes. a few 3000 "different" enzymes should be coated. Fre quently enzymes with very diversified homes are incorporated lower than an identical EC quantity. even supposing we intend to offer a consultant review at the char acteristics and variability of every enzyme the guide isn't really a compendium. The reader must visit the first literature for extra distinctive info. evidently it isn't attainable to hide all of the various literature references for every enzyme (for unique enzymes as much as 40000) if the information illustration is to be concise as is intended.
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Extra resources for Enzyme Handbook 10: Class 1.1: Oxidoreductases
E. e. e. 161 Systematic name 5beta-Gholestane-3alpha,7alpha, 12alpha,26-tetraol:NAD+ 26-oxidoreductase Recommended name Cholestanetetraol 26-dehydrogenase Synonymes Dehydrogenase, cholestanetetrol 265beta-Gholestane-3 alpha,7alpha, 12alpha,26-tetrol dehydrogenase  TEHC-NAD oxidoreductase  CAS Reg. No. : Biochim. Biophys. : J. BioI. : Biochem. Biophys. Res. 162 Systematic name Erythritol:NADP+ oxidoreductase Recommended name Erythrulose reductase Synonymes Reductase, D-erythrulose D-Erythrulose reductase D-Threitol:NADP+ oxidoreductase (in reference 2 the enzymatic reaction product of D-erythrulose is incorrectly identified as erythritol, gas-liquid and thin-layer chromatographic data have confirmed the product to be D-threitol, not erythritol, for this reason the systematic name D-threitol:NADP+ oxidoreductase should be used instead of erythritol:NADP+ oxidoreductase which has been designated by the IUB Enzyme commision)  CAS Reg.
Ferment. : Biochim. Biophys. : Biochem. , Sherrod, JA: J. : Biochim. Biophys. : Biochim. Biophys. 160 Systematic name (+ ,-)-5-[(tert-Butylamino )-2'-hydroxypropoxy]-1 ,2,3,4-tetrahydro-1-naphthol: NADP+ oxidoreductase Recommended name Dihydrobunolol dehydrogenase Synonymes Dehydrogenase, dihydrobunolol Bunolol reductase CAS Reg. No. e. e. e. 161 Systematic name 5beta-Gholestane-3alpha,7alpha, 12alpha,26-tetraol:NAD+ 26-oxidoreductase Recommended name Cholestanetetraol 26-dehydrogenase Synonymes Dehydrogenase, cholestanetetrol 265beta-Gholestane-3 alpha,7alpha, 12alpha,26-tetrol dehydrogenase  TEHC-NAD oxidoreductase  CAS Reg.
157 Systematic name (S)-3-Hyd roxybutanoyl-CoA: NADP+ oxi dored uctase Recommended name 3-Hydroxybutyryl-CoA dehydrogenase Synonymes beta-Hydroxy butyryl coenzyme A dehydrogenase L( + )-3-Hydroxybutyryl-CoA dehydrogenase [8) BHBD [11) Dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate) L-( + )-3-Hydroxybutyryl-CoA dehydrogenase beta-Hydroxybutyryl-CoA dehydrogenase CAS Reg. No. 157 Subunits Octamer (8 x 26000, Clostridium kluyveri, SOS-PAGE)  Glycoprotein/Lipoprotein 4 ISOLATION/PREPARATION Source organism Clostridium pasteurianum ; Clostridium butylicum ; Clostridium butyricum ; Clostridium tetanomorphum ; Clostridium roseum ; Clostridium rubrum ; Clostridium kluyveri (NAO+ dependent activity and NAOP+ dependent activity ) [1,2,7-9]; Rat [4, 10]; Clostridium acetobutylicum [3, 11]; Oasytricha ruminantium ; Butyriovibrio fibrisolvens  Source tissue Liver [4, 10] Localisation in source Peroxisomes (core) ; Mitochondria (distribution in)  Purification Clostridium kluyveri (simultaneous single-step purification ) [1, 2, 8] Crystallization Cloned [ 11] Renaturated 5 STABILITY pH Temperature (0C) 45 (50% loss of activity after 50 min (NAOP+-dependent activity), 80% loss of activity after 20 min (NAO+-dependent activity))  Enzyme Handbook © Springer-Verlag Berlin Heidelberg 1995 Duplication.
Enzyme Handbook 10: Class 1.1: Oxidoreductases by Professor Dr. Dietmar Schomburg, Dr. Dörte Stephan (auth.), Professor Dr. Dietmar Schomburg, Dr. Dörte Stephan (eds.)