Dietmar Schomburg / Ida Schomburg (eds.)

Class 1 Oxidoreductases IX

EC 1.6 - 1.8
Herausgeber: Schomburg, Dietmar; Schomburg, Ida, Mitarbeit: Chang, Antje; Herausgegeben von Schomburg, Dietmar; Schomburg, Ida

• Gebundenes Buch

Produktbeschreibung

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.

Produktdetails

• Springer Handbook of Enzymes Nr.24
• Verlag: Springer, Berlin
• Artikelnr. des Verlages: 11331551
• 2. Aufl.
• Seitenzahl: 744
• Erscheinungstermin: 20. Mai 2005
• Englisch
• Abmessung: 241mm x 160mm x 46mm
• Gewicht: 1267g
• ISBN-13: 9783540238553
• ISBN-10: 3540238557
• Artikelnr.: 21142032

Autorenporträt

Dietmar Schomburg, Universität zu Köln / Ida Schomburg, Universität zu Köln

Inhaltsangabe

NAD(P)+ Transhydrogenase (B-specific).- NAD(P)+ Transhydrogenase (AB-specific).- NADH2 Cytochrome c reductase.- Cytochrome-b5 reductase.- Cytochrome reductase (NADPH).- NADPH-Ferrihemoprotein reductase.- NADPH-Cytochrome-c2 reductase.- Leghemoglobin reductase.- NADPH Oxidase.- Cystine reductase (NADH).- Glutathione reductase (NADPH).- Dihydrolipoamide reductase (NAD+).- Protein-disulfide reductase [NAD(P)H].- Thioredoxin reductase (NADPH).- CoA-Glutathione reductase (NADPH).- Asparagusate reductase (NADH).- Trypanothione reductase.- Bis-?-glutamylcystine reductase (NADPH).- CoA-Disulfide reductase (NADH).- Quinone reductase.- Menadione reductase.- NADH Dehydrogenase (ubiquinone).- Monodehydroascorbate reductase (NADH).- NADPH:Quinone reductase.- p-Benzoquinone reductase (NADPH).- 2-Hydroxy-1,4-benzoquinone reductase.- Nitrate reductase (NADH).- Nitrate reductase [NAD(P)H].- Nitrate reductase (NADPH).- Nitrite reductase [NAD(P)H].- Nomenclature.- Hyponitrite reductase.- Azobenzene reductase.- GMP Reductase.- Trimethylamine-N-oxide reductase.- Nitroquinoline-N-oxide reductase.- Hydroxylamine reductase (NADH).- 4-(Dimethylamino)phenylazoxybenzene reductase.- N-Hydroxy-2-acetamidofluorene reductase.- Ferredoxin-NADP+ reductase.- Rubredoxin-NAD+ reductase.- NAD(P)H Dehydrogenase (FMN).- NADPH Dehydrogenase (flavin).- NADPH Dehydrogenase.- NAD(P)H Dehydrogenase (quinone).- NADH Dehydrogenase.- Nitrite reductase.- NADH Dehydrogenase (quinone).- NADPH Dehydrogenase (quinone).- Dihydropteridine reductase.- Aquacobalamin reductase.- Cob(ll)alamin reductase.- Dihydropteridine reductase (NADH).- Aquacobalamin reductase (NADPH).- Cyanocobalamin reductase (NADPH, cyanide-eliminating).- Ferric-chelate reductase.- Nitrate reductase (NADH).- Nitrate reductase [NAD(P)H].- Nitrate reductase (NADPH).- Nitrite reductase [NAD(P)H].- Hyponitrite reductase.- Azobenzene reductase.- GMP Reductase.- Nomenclature.- Nitroquinoline-N-oxide reductase.- Hydroxylamine reductase (NADH).- 4-(Dimethylamino)phenylazoxybenzene reductase.- N-Hydroxy-2-acetamidofluorene reductase.- Nitrite reductase (NO-forming).- Nitrite reductase (cytochrome; ammonia-forming).- Trimethylamine-N-oxide reductase (cytochrome c).- Nitroethane oxidase.- Acetylindoxyl oxidase.- Urate oxidase.- Hydroxylamine oxidase.- 3-Aci-nitropropanoate oxidase.- Ferredoxin-nitrite reductase.- Ferredoxin-nitrate reductase.- Hydroxylamine reductase.- Nitric-oxide reductase.- Nitrite reductase.- Nitrate reductase.- 5,10-Methylenetetrahydrofolate reductase (FADH2).- Nitrous-oxide reductase.- Nitric-oxide reductase.- Cysteamine dehydrogenase.- Sulfite reductase (NADPH).- Hypotaurine dehydrogenase.- Dihydrolipoamide dehydrogenase.- 2-Oxopropyl-CoM reductase (carboxylating).- Cystine reductase.- Glutathione-disulfide reductase.- Protein-disulfide reductase.- Thioredoxin-disulfide reductase.- CoA-Glutathione reductase.- Asparagusate reductase.- Trypanothione-disulfide reductase.- Bis-?-glutamylcystine reductase.- CoA-Disulfide reductase.- Mycothione reductase.- Sulfite dehydrogenase.- Thiosulfate dehydrogenase.- Nomenclature.- Sulfite oxidase.- Thiol oxidase.- Glutathione oxidase.- Methanethiol oxidase.- Prenylcysteine oxidase.- Glutathione-homocystine transhydrogenase.- Protein-disulfide reductase (glutathione).- Glutathione-CoA-glutathione transhydrogenase.- Glutathione-cystine transhydrogenase.- Methionine-S-oxide reductase.- Protein-methionine-S-oxide reductase.- Enzyme-thiol transhydrogenase (glutathione-disulfide).- Phosphoadenylyl-sulfate reductase (thioredoxin).- Adenylyl-sulfate reductase (glutathione).- Adenylyl-sulfate reductase (thioredoxin).- Glutathione dehydrogenase (ascorbate).- Nitrate-ester reductase.- Sulfite reductase (ferredoxin).- Sulfite reductase.- Adenylyl-sulfate reductase.- Hydrogensulfite reductase.- Phosphoadenosine-phosphosulfate reductase.

Rezensionen

"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