Class 3 Hydrolases: EC 3.4.22-3.13

by Dietmar Schomburg (Editor), Ida Schomburg (Editor)

Overview

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.

Product Details

ISBN-13:	9783662502181
Publisher:	Springer Berlin Heidelberg
Publication date:	08/23/2016
Series:	Springer Handbook of Enzymes , #6
Edition description:	Softcover reprint of the original 2nd ed. 2009
Pages:	572
Product dimensions:	6.10(w) x 9.25(h) x 0.05(d)

Table of Contents

Gingipain K.- Staphopain.- Separase.- V-Cath endopeptidase.- Cruzipain.- Calpain-1.- Calpain-2.- Calpain-3.- Caspase-2.- Caspase-3.- Caspase-4.- Caspase-5.- Caspase-6.- Caspase-7.- Caspase-8.- Caspase-9.- Caspase-10.- Caspase-11.- Peptidase 1 (mite).- Calicivirin.- Zingipain.- Ulp1 Peptidase.- Memapsin 1.- Memapsin 2.- HIV-2 retropepsin.- Plasminogen activator Pla.- Omptin.- GPR endopeptidase.- Pappalysin-1.- Membrane-type matrix metalloproteinase-1.- ADAM10 Endopeptidase.- ADAMTS-4 endopeptidase.- Anthrax lethal factor endopeptidase.- Ste24 endopeptidase.- S2P endopeptidase.- ADAM 17 endopeptidase.- Adenosylcobinamide hydrolase.- N-Substituted formamide deformylase.- Pantetheine hydrolase.- Glutaryl-7-aminocephalosporanic-acid acylase.-—-Glutamyl-?-aminobutyrate hydrolase.- N-Malonylurea hydrolase.- Succinylglutamate desuccinylase.- Acyl-homoserine-lactone acylase.- Histone deacetylase.- Hydroxyisourate hydrolase.- Enamidase.- Proclavaminate amidinohydrolase.- N-Succinylarginine dihydrolase.- GTP Cyclohydrolase IIa.- dCTP deaminase (dUMP-forming).- Glycerol-3-phosphate-transporting ATPase.- Sulfate-transporting ATPase.- Heterotrimeric G-protein GTPase.- Small monomeric GTPase.- Protein-synthesizing GTPase.- Signal-recognition-particle GTPase.- Dynamin GTPase.- Tubulin GTPase.- (R)-2-Haloacid dehalogenase.- 2-Haloacid dehalogenase (configuration-inverting).- 2-Haloacid dehalogenase (configuration-retaining).- Phosphonopyruvate hydrolase.- UDP-sulfoquinovose synthase.- 5-Deoxyribos-5-ylhomocysteinase.- 2'-Hydroxybiphenyl-2-sulfinate desulfinase.

Editorial Reviews

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)

From the Publisher