Class 1 Oxidoreductases X (eBook, PDF)

EC 1.9 - 1.13
Redaktion: Schomburg, Dietmar; Schomburg, Ida

• Format: PDF

Produktbeschreibung

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.

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Produktdetails

• Verlag: Springer Berlin Heidelberg
• Seitenzahl: 749
• Erscheinungstermin: 25. Oktober 2007
• Englisch
• ISBN-13: 9783540377047
• Artikelnr.: 37366279

Autorenporträt

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

Inhaltsangabe

Cytochrome-c oxidase.- Pseudomonas cytochrome oxidase.- Nitrate reductase (cytochrome).- Iron-cytochrome-c reductase.- trans-Acenaphthene-l,2-diol dehydrogenase.- l-Ascorbate-cytochrome-b5 reductase.- Ubiquinol-cytochrome-c reductase.- Catechol oxidase.- Laccase.- l-Ascorbate oxidase.- o-Aminophenol oxidase.- 3-Hydroxyanthranilate oxidase.- Rifamycin-B oxidase.- Sulochrin oxidase [(+)-bisdechlorogeodin-forming].- Sulochrin oxidase [(-)-bisdechlorogeodin-forming].- Plastoquinol-plastocyanin reductase.- NADH peroxidase.- NADPH peroxidase.- Fatty-acid peroxidase.- Recommended name never specified.- Cytochrome-c peroxidase.- Catalase.- Peroxidase.- Iodide peroxidase.- Glutathione peroxidase.- Chloride peroxidase.- L-Ascorbate peroxidase.- Phospholipid-hydroperoxide glutathione peroxidase.- Manganese peroxidase.- Diarylpropane peroxidase.- Peroxidase.- Hydrogen dehydrogenase.- Hydrogen dehydrogenase (NADP+).- Cytochrome-c3 hydrogenase.- Hydrogen:quinone oxidoreductase.- Ferredoxin hydrogenase.- Ferredoxin hydrogenase.- Coenzyme F420 hydrogenase.- N5,N10-Methenyltetrahydromethanopterin hydrogenase.- Methanosarcina-phenazine hydrogenase.- Coenzyme F420 hydrogenase.- Coenzyme-M-7-mercaptoheptanoylthreoninephosphate-heterodisulfide hydrogenase.- Hydrogen:quinone oxidoreductase.- N5,N10-Methenyltetrahydromethanopterin hydrogenase.- 3,4-Dihydroxyquinoline 2,4-dioxygenase.- Hydrogenase (acceptor).- Catechol 1,2-dioxygenase.- Catechol 2,3-dioxygenase.- Protocatechuate 3,4-dioxygenase.- Gentisate 1,2-dioxygenase.- Homogentisate 1,2-dioxygenase.- 3-Hydroxyanthranilate 3,4-dioxygenase 1.1 3.11.6.- 3,4-Dihydroxyphenylacetate 3,4-dioxygenase.- Protocatechuate 4,5-dioxygenase.- 2,5-Dihydroxypyridine 5,6-dioxygenase.- 7,8-Dihydroxykynurenate 8,8a-dioxygenase.- Tryptophan 2,3-dioxygenase.-Lipoxyge nase.- Ascorbate 2,3-dioxygenase.- 2,3-Dihydroxybenzoate 3,4-dioxygenase.- 3,4-Dihydroxyphenylacetate 2,3-dioxygenase.- 3-Carboxyethylcatechol 2,3-dioxygenase.- Indole 2,3-dioxygenase.- Sulfur dioxygenase.- Cysteamine dioxygenase.- Cysteine dioxygenase.- ?-Carotene 15,15?-dioxygenase.- Caffeate 3,4-dioxygenase.- 2,3-Dihydroxyindole 2,3-dioxygenase.- Quercetin 2,3-dioxygenase.- 3,4-Dihydroxy-9,10-secoandrosta-1,3,5(10)- triene-9,17-dione 4,5-dioxygenase.- Peptide-tryptophan 2,3-dioxygenase.- 4-Hydroxyphenylpyruvate dioxygenase.- 2,3-Dihydroxybenzoate 2,3-dioxygenase.- Stizolobate synthase.- Stizolobinate synthase.- Arachidonate 12-lipoxygenase.- 2-Nitropropane dioxygenase.- Arachidonate 15-lipoxygenase.- Arachidonate 5-lipoxygenase.- Pyrogallol 1,2-oxygenase.- Chloridazon-catechol dioxygenase.- Hydroxyquinol 1,2-dioxygenase.- 1-Hydroxy-2-naphthoate 1,2-dioxygenase.- Biphenyl-2,3-diol 1,2-dioxygenase.- Arachidonate 8-lipoxygenase.- 2,4?-Dihydroxyacetophenone dioxygenase.- Indoleamine-pyrrole 2,3-dioxygenase.- Lignostilbene ? ?-dioxygenase.- Linoleate diol synthase.- Linoleate 11-lipoxygenase.- 4-Hydroxymandelate synthase.- 3-Hydroxy-4-oxoquinoline 2,4-dioxygenase.- 3-Hydroxy-2-methylquinolin-4-one 2,4- dioxygenase.- Chlorite O2-lyase.- Acetylacetone-cleaving enzyme.- Arginine 2-monooxygenase.- Lysine 2-monooxygenase.- Tryptophan 2-monooxygenase.- Lactate 2-monooxygenase.- Renilla-luciferin 2-monooxygenase.- Cypridina-luciferin 2-monooxygenase.- Photinus-luciferin 4-monooxygenase (ATP-hydrolysing).- Watasenia-luciferin 2-monooxygenase.- Phenylalanine 2-monooxygenase.- Lysine 6-monooxygenase.- Methylphenyltetrahydropyridine N-monooxygenase.- apo-?-Carotenoid-14',13'-dioxygenase.- Inositol oxygenase.- Benzoate 1,2-dioxygenase.- Tryptophan2?-dioxygenase.- 4-Chlorophenylacetate 3,4-dioxygenase.- 3,4-Dihydroxyquinoline 2,4-dioxygenase.

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