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Springer Handbook of Enzymes provides data on enzymes sufficiently well characterized. It offers concise and complete descriptions of some 5,000 enzymes and their application areas. Data sheets are arranged in their EC-Number sequence and the volumes themselves are arranged according to enzyme classes.
This new, second edition reflects considerable progress in enzymology: many enzymes are newly classified or reclassified. Each entry is correlated with references and one or more source organisms. New datafields are created: application and engineering (for the properties of enzymes where the sequence has been changed). The total amount of material contained in the Handbook has more than doubled so that the complete second edition consists of 39 volumes as well as a Synonym Index. In addition, starting in 2009, all newly classified enzymes are treated in Supplement Volumes.
Springer Handbook of Enzymes is an ideal source of information for researchers in biochemistry, biotechnology, organic and analytical chemistry, and food sciences, as well as for medicinal applications.
List of contents
Phosphorylase.- Dextrin dextranase.- Amylomaltase.- Amylosucrase.- Dextransucrase.- Maltose 3-glycosyltransferase.- Sucrose phosphorylase.- Maltose phosphorylase.- Inulosucrase.- Levansucrase.- Glycogen (starch) synthase.- Cellulose synthase (UDP-forming).- Sucrose synthase.- Sucrose-phosphate synthase.- ?,?-Trehalose-phosphate synthase (UDP-forming).- Chitin synthase.- Glucuronosyltransferase.- 1,4-?-Glucan branching enzyme.- Cyclomaltodextrin glucanotransferase.- Cellobiose phosphorylase.- Starch synthase.- Lactose synthase.- Sphingosine ?-galactosyltransferase.- 1,4-?-Glucan 6-?-glucosyltransferase.- 4-?-Gluca notransferase.- DNA ?-glucosyltransferase.- DNA ?-glucosyltransferase.- Glucosyl-DNA ?-glucosyltransferase.- Cellulose synthase (GDP-forming).- 1,3-?-Oligoglucan phosphorylase.- Laminaribiose phosphorylase.- Glucomannan 4-?-mannosyltransferase.- Alginate synthase.- 1,3-?-Glucan synthase.- Phenol ?-glucosyltransferase.- ?,?-Trehalose-phosphate synthase (GDP-forming).- Fucosylgalactoside 3-?-galactosyltransferase.- ?-N-Acetylglucosaminylglycopeptide ?-1,4-galactosyltransferase.- Steroid N-acetylglucosaminyltransferase.- Glycoprotein-fucosylgalactoside ?-N-acetylgalactosaminyltransferase.- Polypeptide N-acetylgalactosaminyltransferase.- UDPglucuronate-estriol 17 ?-d- glucuronosyltransferase.- Polygalacturonate 4-?-galactu ronosyltransferase.- Lipopolysaccharide 3-?-galactosyltransferase.- 2-Hydroxyacylsphingosine 1-?-galactosyltransferase.- 1,2-Diacylglycerol 3-?-galactosyltransferase.- N-Acylsphingosine galactosyltransferase.- Heteroglycan ?-mannosyltransferase.- Cellodextrin phosphorylase.- Procollagen galactosyltransferase.- UDP-N-Acetylglucosamine-glycoprotein N-acetylglucosaminyltransferase.- Poly(glycerol-phosphate)?-glucosyltransferase.- Poly(ribitol-phosphate) ?-glucosyltransferase.- Undecaprenyl-phosphate mannosyltransferase.- Teichoic-acid synthase.- Lipopolysaccharide N-acetylglucosaminyltransferase.- Phosphatidyl-myo-inositol ?-mannosyltransferase.- Lipopolysaccharide glucosyltransferase I.- UDPglucuronate-estradiol glucuronosyltransferase.- Abequosyltransferase.- UDPglucuronate-estriol 16?- glucuronosyltransferase.- Ganglioside galactosyltransferase.- Linamarin synthase.- ?,?-Trehalose phosphorylase.- 3-GalactosyI-N-acetylglucosaminide 4-?-L-fucosyltransferase.- Procollagen glucosyltransferase.- Galactinol-raffinose galactosyltransferase.- Glycoprotein 6-?-l-fucosyltransferase.- Galactoside 2-?-l-fucosyltransferase.- Poly(ribitol-phosphate) N-acetylglucosaminyltransferase.- Arylamine glucosyltransferase.- 1,4-?-Xylan synthase.- Lipopolysaccharide glucosyltransferase II.- Glycosaminoglycan galactosyltransferase.- UDP-Galacturonosyltransferase.- UDPglucuronate-bilirubin glucuronosyltransferase.- UDPglucuronate-bilirubin-glucuronoside glucuronosyltransferase.- Phosphopolyprenol glucosyltransferase.- Galactosylgalactosylglucosylceramide ?-d-acetylgalactosaminyltransferase.- Ceramide glucosyltransferase.- Flavone 7-O-?-glucosyltransferase.- Galactinol-sucrose galactosyltransferase.- Dolichyl-phosphate ?-d-mannosyltransferase.- U DPglucuronate-1,2-diacylglycerol glucuronosyltransferase.- Cyanohydrin ?-glucosyltransferase.- Glucosaminylgalactosylglucosylceramide ?-galactosyltransferase.- ?-d-GalactosyI-N- acetylglucosaminylglycopeptide ?-1,3-galactosyltransferase.- Globoside ?-N-acetylgalactosaminyltransferase.- Galactosylglucosaminylgalactosylglucosylceramide ?-l-fucosyltransferase.
Summary
Springer Handbook of Enzymes offers concise and complete descriptions of some 5,000 enzymes, each sufficiently well characterized. Their application in analytical, synthetic and biotechnology processes as well as in food industry, and for medicinal treatments is added.
This new, second edition reflects considerable progress in enzymology: many enzymes are newly classified or reclassified. Each entry is correlated with references and one or more source organisms. New datafields are created: application and engineering. The total amount of material contained in the Handbook has more than doubled so that the complete second edition consists of 39 volumes as well as a synonym index. Starting in 2009, all newly classified enzymes are treated in Supplement Volumes.
Additional text
ChemBioChem 3/2002: Comparing Volume 2 of the first edition with Volume 1 of the second edition one rapidly notices that an incredible amount of work was spent on updating the different datafields.
The handbook is definitely worth buying, since it is probably the best reference manual available to date and is, therefore, an improtant acquisition for libraries. (W. Kroutil, University of Graz)
Report
ChemBioChem 3/2002: Comparing Volume 2 of the first edition with Volume 1 of the second edition one rapidly notices that an incredible amount of work was spent on updating the different datafields.
The handbook is definitely worth buying, since it is probably the best reference manual available to date and is, therefore, an improtant acquisition for libraries. (W. Kroutil, University of Graz)
