Class 3・Hydrolases
Author(s)
Bibliographic Information
Class 3・Hydrolases
（Springer handbook of enzymes / Dietmar Schomburg, Ida Schomburg (eds.), Suppl. v. S5-S6）
Springer, c2009
2nd ed
- S5
- S6
Available at / 12 libraries
-
University Library for Agricultural and Life Sciences, The University of Tokyo図
S5464.5:Sc6:2nd ed-S55010463387,
S6464.5:Sc6:2nd ed-S65010463395 -
Hokkaido University, Faculty and Graduate School of Engineering図書
S5572.7/SP833580106626,
S6572.7/SP833580119688 -
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Note
"The first edition was published as the 'Enzyme Handbook' edited by D. and I. Schomburg"--T.p. verso
S5. EC 3.1-3.4.21 -- S6. EC 3.4.22-3.13
Includes bibliographical references
Description and Table of Contents
- Volume
-
S5 ISBN 9783540857020
Description
The Springer Handbook of Enzymes provides concise data on some 5,000 enzymes sufficiently well characterized - and here is the second, updated edition. Their application in analytical, synthetic and biotechnology processes as well as in food industry, and for medicinal treatments is added. Data sheets are arranged in their EC-Number sequence. The new edition reflects considerable progress in enzymology: the total material has more than doubled, and the complete 2nd edition consists of 39 volumes plus Synonym Index. Starting in 2009, all newly classified enzymes are treated in Supplement Volumes.
Table of Contents
Polyneuridine-aldehyde esterase.- Hormone-sensitive lipase.- Acetylajmaline esterase.- Quorum-quenching N-acyl-homoserine lactonase.- Pheophorbidase.- Phenylacetyl-CoA hydrolase.- Bile-acid-CoA hydrolase.- Choloyl-CoA hydrolase.- Mannosyl-3-phosphoglycerate phosphatase.- 2-Phosphosulfolactate phosphatase.- 5-Phytase.- ?-Ribazole phosphatase.- Pyridoxal phosphatase.- Phosphoethanolamine/phosphocholine phosphatase.- Lipid-phosphate phosphatase.- Acireductone synthase.- Cyclic-guanylate-specific phosphodiesterase.- Ribonuclease D.- tRNase Z.- Oligoxyloglucan reducing-end-specific cellobiohydrolase.- Xyloglucan-specific endo-?-1,4-glucanase.- Mannosylglycoprotein endo-?-mannosidase.- Fructan ?-(2,1)-fructosidase.- Fructan ?-(2,6)-fructosidase.- Xyloglucan-specific exo-?-1,4-glucanase.- Oligosaccharide reducing-end xylanase.- ?-carrageenase.- ?-Agarase.- ?-Neoagaro-oligosaccharide hydrolase.- Xyloglucan-specific exo-?-1,4-glucanase.- ?-Apiosyl-?-glucosidase.- ?-carrageenase.- 1,6-?-d-Mannosidase.- Galactan endo-1,6-?-galactosidase.- N-Methyl nucleosidase.- Microsomal epoxide hydrolase.- Soluble epoxide hydrolase.- Cholesterol-5,6-oxide hydrolase.- PepB Aminopeptidase.- d-Ala-d-Ala dipeptidase.- Xaa-Xaa-Pro Tripeptidyl-peptidase.- Cyanophycinase.- Physarolisin.- Mannan-binding lectin-associated serine protease-2.- Rhomboid protease.- Hepsin.- Peptidase Do.- HtrA2 Peptidase.- Matriptase.- C5a Peptidase.- Aqualysin 1.- Site-1 protease.- Pestivirus NS3 polyprotein peptidase.- Equine arterivirus serine peptidase.- Infectious pancreatic necrosis birnavirus Vp4 peptidase.- SpolVB peptidase.- Stratum corneum chymotryptic enzyme.- Kallikrein 8.- Kallikrein 13.- Oviductin.
- Volume
-
S6 ISBN 9783540857044
Description
The Springer Handbook of Enzymes provides concise data on some 5,000 enzymes sufficiently well characterized - and here is the second, updated edition. Their application in analytical, synthetic and biotechnology processes as well as in food industry, and for medicinal treatments is added. Data sheets are arranged in their EC-Number sequence. The new edition reflects considerable progress in enzymology: the total material has more than doubled, and the complete 2nd edition consists of 39 volumes plus Synonym Index. Starting in 2009, all newly classified enzymes are treated in Supplement Volumes.
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.
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