Buch, Englisch, Band S5, 462 Seiten, HC runder Rücken kaschiert, Format (B × H): 160 mm x 241 mm, Gewicht: 887 g
Reihe: Springer Handbook of Enzymes
EC 3.1-3.4.21
Buch, Englisch, Band S5, 462 Seiten, HC runder Rücken kaschiert, Format (B × H): 160 mm x 241 mm, Gewicht: 887 g
Reihe: Springer Handbook of Enzymes
ISBN: 978-3-540-85702-0
Verlag: Springer Berlin Heidelberg
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.
Zielgruppe
Research
Fachgebiete
- Naturwissenschaften Chemie Organische Chemie Biochemie
- Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Vorklinische Medizin: Grundlagenfächer Biochemie (med.)
- Naturwissenschaften Biowissenschaften Mikrobiologie
- Naturwissenschaften Biowissenschaften Enzymologie
- Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
- Interdisziplinäres Wissenschaften Wissenschaften Interdisziplinär Ökotrophologie (Ernährungs- und Haushaltswissenschaften)
- Technische Wissenschaften Verfahrenstechnik | Chemieingenieurwesen | Biotechnologie Biotechnologie
Weitere Infos & Material
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.