Download Enzyme Handbook by Dietmar Schomburg, Margit Salzmann (auth.) PDF

By Dietmar Schomburg, Margit Salzmann (auth.)

ISBN-10: 364248963X

ISBN-13: 9783642489631

ISBN-10: 364276729X

ISBN-13: 9783642767296

Enzymes are utilized in natural synthesis and in analytical chemistry, in commercial construction approaches of prescribed drugs and in foodstuff processing. discovering an appropriate enzyme for a wanted transformation or with a de- fined specificity isn't really regularly a simple job. greater than 3000 enzymes are good defined up to now. The Enzyme Handbook offers all of the details for choosing the correct enzyme to accomplish outlined differences in a given surroundings. The Enzyme Handbook devotes a variable variety of pages for every enzyme, looking on the volume of knowledge to be had with the EC quantity as ordering criterion inside a quantity. Revised information sheets may be published for person enzymes and newly characterised enzymes and so they can simply be looked after into the binders on the acceptable position. every one info sheet is split into 7 sections: - Nomenclature (EC quantity, Systematic identify, Recom- mended identify, Synonyms, CAS Reg. No.) - Reaction and specificity (Catalysed response, response kind, usual substrates, Substrate spectrum, Product spectrum, Inhibitors, Cofactors/prosthetic teams, steel compounds/salts, Turnover quantity, particular job, KM-value, pH-optimum, pH-range, Tem- perature optimal, Temperature variety) - Enzyme structure (Molecular weight, Subunits, Glyco-/Lipoprotein) - Isolation/Preparation (Source organism, resource tissue, Localisation in resource, Purification, Crystallization, Cloned, Renatured) - Stability (pH, Temperature, Oxidation, natural sol- vent, basic balance info, garage) - Cross-References (to constitution facts Banks) - Literature references

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Biochem. : Eur. J. : Arch. Biochem. -Biol. : Anal. : J. : Eur. J. : Eur. J. : J. Biol. C. 37 (formerly) CASReg. No. 37290-73-6 2 REACTION AND SPECIFICITY Catalysed reaction Trans-2, 3-epoxysuccinate -+ meso-tartrate + H20-+ Reaction type Ether hydro Iysis Naturalsubstrates Trans-2, 3-epoxysuccinate + H2 0 (carbon source) [1] Substrate spectrum 1 Trans-2, 3-epoxysuccinate + H2 0 (0- and L-trans-2, 3-epoxysuccinate) [1] 2 More (acts on both optical isomers of substrate, not: cis-epoxysuccinate) [1] Product spectrum 1 Meso-tartrate 2 ?

Arch. 8iochem. : Biochim. Biophys. : 8iochem. Biophys. Res. : FEMS Microbiol. : Agric. Biol. : Agric. 8iol. : J. Bio I. : Agric. Biol. : Agric. Bio I. : Biochim. Biophys. Acta, 429, 933-949 (1976) [27] Appel, W. in "Methoden Enzym. L. in "The Enzymes", 3rd. Ed. : Arch. 8iochem. : Hoppe-Seyler's Z. Physiol. : Hoppe-Seyler's Z. Physiol. : Hoppe-Seyler's Z. Physiol. : Hoppe-Seyler' S Z. Physiol. : Hoppe-Seyler's Z. Physiol. , Holzer, H. : J. Bio I. 1. 2 (formerly) Aminopeptidase M II L-Aianine aminopeptidase CASReg.

G. 4 Temperature range (0 C) 3 ENZYME STRUCTURE Molecular weight 137200 (pig, tripeptidase-2, Sedimentation equilibrium centrifugation) [13] 108000 (Bacillus stearothermophilus, gel filtration) [11] 6500Q-80000 (guinea pig, gel filtration [2], Macaca fuscata, gel filtration, SOS-PAGE [6], E. coli, gel filtration [9], pig, peptidase-1, sedimentation equilibrium centrifugation [13]) [2, 6, 9, 13] 5000Q-57000 (rabbit, ultracentrifugation, SOS-PAGE) [8] Subunits Dimer (2 x 80900, pig, tripeptidase-2, Sedimentation equilibrium centrifugation in 6 M guanidium chloride + mercaptoethanol [13], 2 x 47500, Bacillus stearothermophilus, SOS-PAGE) [11, 13] Monomer (65000-80000, guinea pig, SOS-PAGE with reducing agents [2], Macaca fuscata, SOS-PAGE [6], pig, peptidease-1, Sedimentation equilibrium centrifugation in 6 M guanidium chloride + mercaptoethanol [13], 1 x 57000, rabbit, SOS-PAGE [8]) [2, 6, 8, 13] Glycoprotei n/Li poprotein Glycoprotein [8]; No glycoprotein [2] 4 ISOLATION/PREPARATION Source organism Guinea pig [1, 2, 7]; Rat [3, 4, 7]; Saccharomyces cerevisiae [5]; Macaca fuscata (japanese monkey) [6]; Rabbit [8]; E.

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