2009, ISBN: 9783642362651
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 … Más…
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ISBN: 9783642362651
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Springer.com Springer Handbook of Enzymes offers complete descriptions of 5,000 enzymes and their applications. Data sheets are arranged in their EC-Number sequence and the volumes themselves are arranged according to enzyme classes. This volume covers Oxidoreductases Gastos de envío:zzgl. Versandkosten., más gastos de envío Details... |
2013, ISBN: 9783642362651
EC 1, eBooks, eBook Download (PDF), Auflage, [PU: Springer-Verlag], [ED: 2], Springer-Verlag, 2013
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2013, ISBN: 9783642362651
EC 1, eBooks, eBook Download (PDF), 2nd ed. 2013, [PU: Springer Berlin Heidelberg], Springer Berlin Heidelberg, 2013
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2013, ISBN: 9783642362651
EC 1, [ED: 2], 2nd ed. 2013, eBook Download (PDF), eBooks, [PU: Springer Berlin Heidelberg]
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2009, ISBN: 9783642362651
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 … Más…
ISBN: 9783642362651
Life Sciences; Biochemistry, general; Molecular Medicine; Pharmacology/Toxicology; Food Science; Biotechnology; Veterinary Medicine/Veterinary Science Applied Microbiology, Biochemistry, … Más…
2013
ISBN: 9783642362651
EC 1, eBooks, eBook Download (PDF), Auflage, [PU: Springer-Verlag], [ED: 2], Springer-Verlag, 2013
2013, ISBN: 9783642362651
EC 1, eBooks, eBook Download (PDF), 2nd ed. 2013, [PU: Springer Berlin Heidelberg], Springer Berlin Heidelberg, 2013
2013, ISBN: 9783642362651
EC 1, [ED: 2], 2nd ed. 2013, eBook Download (PDF), eBooks, [PU: Springer Berlin Heidelberg]
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Detalles del libro - Class 1 Oxidoreductases
EAN (ISBN-13): 9783642362651
ISBN (ISBN-10): 3642362656
Año de publicación: 2013
Editorial: Springer-Verlag
714 Páginas
Idioma: eng/Englisch
Libro en la base de datos desde 2012-07-14T08:49:40+02:00 (Madrid)
Página de detalles modificada por última vez el 2024-01-19T07:06:34+01:00 (Madrid)
ISBN/EAN: 9783642362651
ISBN - escritura alterna:
3-642-36265-6, 978-3-642-36265-1
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Autor del libro: chang, chan, antje, schomburg, schöm
Título del libro: cla, class
Datos del la editorial
Autor: Dietmar Schomburg; Ida Schomburg; Antje Chang
Título: Springer Handbook of Enzymes; Class 1 Oxidoreductases - EC 1
Editorial: Springer; Springer Berlin
714 Páginas
Año de publicación: 2013-04-01
Berlin; Heidelberg; DE
Idioma: Inglés
309,23 € (DE)
317,90 € (AT)
354,00 CHF (CH)
Available
XIX, 714 p.
EA; E107; eBook; Nonbooks, PBS / Biologie/Biochemie, Biophysik; Biochemie; Verstehen; Applied Microbiology; Biochemistry; Biotransformation; Enzymes; Food Science; Molecular Medicine; Oxidoreductases; B; Biochemistry; Biomedical Research; Pharmacology; Food Science; Biotechnology; Veterinary Science; Biomedical and Life Sciences; Medizinische Forschung; Pharmakologie; Lebensmittel- und Getränketechnologie; Biotechnologie; Tiermedizin; BB
1.1.1.295 momilactone-A synthase.- 1.1.1.296 dihydrocarveol dehydrogenase.- 1.1.1.297 limonene-1,2-diol dehydrogenase .- 1.1.1.298 3-hydroxypropionate dehydrogenase (NADP+) .- 1.1.1.299 malate dehydrogenase [NAD(P)+].- 1.1.1.300 NADP-retinol dehydrogenase .- 1.1.1.301 D-arabitol-phosphate dehydrogenase.- 1.1.1.302 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5’-phosphate reductase .- 1.1.1.303 diacetyl reductase [(R)-acetoin forming].- 1.1.1.304 diacetyl reductase [(S)-acetoin forming].- 1.1.1.305 UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating) .- 1.1.1.306 S-(hydroxymethyl)mycothiol dehydrogenase.- 1.1.1.307 D-xylose reductase.- 1.1.1.308 sulfopropanediol 3-dehydrogenase.- 1.1.1.309 phosphonoacetaldehyde reductase (NADH) .- 1.1.2.6 polyvinyl alcohol dehydrogenase (cytochrome) .- 1.1.2.7 methanol dehydrogenase (cytochrome c).- 1.1.2.8 alcohol dehydrogenase (cytochrome c) .- 1.1.5.3 glycerol-3-phosphate dehydrogenase .- 1.1.5.4 malate dehydrogenase(quinone).- 1.1.5.5 alcohol dehydrogenase (quinone) .- 1.1.5.6 formate dehydrogenase-N.- 1.1.5.7 cyclic alcohol dehydrogenase (quinone).- 1.1.5.8 quinate dehydrogenase (quinone).- 1.1.99.1 alcohol dehydrogenase (azurin).- 1.1.99.33 formate dehydrogenase (acceptor) .- 1.1.99.34 glucose-6-phosphate dehydrogenase (coenzyme-F420) .- 1.1.99.35 soluble quinoprotein glucose dehydrogenase .- 1.1.99.36 NDMA-dependent alcohol dehydrogenase.- 1.1.99.37 NDMA-dependent methanol dehydrogenase.- 1.2.1.73 sulfoacetaldehyde dehydrogenase.- 1.2.1.74 abietadienal dehydrogenase .- 1.2.1.75 malonyl CoA reductase (malonate semialdehyde-forming).- 1.2.1.76 succinate-semialdehyde dehydrogenase (acylating).- 1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) .- 1.2.1.78 2-formylbenzoate dehydrogenase .- 1.2.1.80 long-chain acyl-[acyl-carrier-protein] reductase .- 1.2.5.1 pyruvate dehydrogenase (quinone).- 1.3.1.81 (+)-pulegone reductase.- 1.3.1.82 (-)-isopiperitenone reductase .- 1.3.1.83 geranylgeranyl diphosphate reductase .- 1.3.1.84 acrylyl-CoA reductase (NADPH) .- 1.3.1.85 crotonyl-CoA carboxylase/reductase .- 1.3.1.86 crotonyl-CoA reductase.- 1.3.5.2 dihydroorotate dehydrogenase (quinone) .- 1.3.5.3 protoporphyrinogen IX dehydrogenase (menaquinone) .- 1.3.5.4 fumarate reductase (menaquinone) .- 1.3.7.6 phycoerythrobilin synthase .- 1.3.99.24 2-amino-4-deoxychorismate dehydrogenase .- 1.3.99.25 carvone reductase.- 1.4.3.21 primary-amine oxidase.- 1.4.3.22 diamine oxidase.- 1.4.3.23 7-chloro-L-tryptophan oxidase.- 1.4.5.1 D-amino acid dehydrogenase (quinone).- 1.5.3.13 N1-acetylpolyamine oxidase.- 1.5.3.14 polyamine oxidase (propane-1,3-diamineforming).- 1.5.3.15 N8-acetylspermidine oxidase (propane-1,3-diamine-forming).- 1.5.3.16 spermine oxidase .- 1.5.3.17 non-specific polyamine oxidase .- 1.5.99.13 D-proline dehydrogenase.- 1.7.5.1 nitrate reductase (quinone) .- 1.8.1.16 glutathione amide reductase .- 1.8.7.2 ferredoxin:thioredoxin reductase .- 1.11.1.17 glutathione amide-dependent peroxidase.- 1.11.1.19 dye decolorizing peroxidase.- 1.11.2.1 unspecific peroxygenase.- 1.13.11.56 1,2-dihydroxynaphthalene dioxygenase monooxygenase.- 1.14.13.112 3-epi-6-deoxocathasterone 23-monooxygenase.- 1.14.13.113 FAD-dependent urate hydroxylase .- 1.14.13.114 6-hydroxynicotinate 3-monooxygenase .- 1.14.13.115 angelicin synthase.- 1.14.13.116 geranylhydroquinone 3’’-hydroxylase.- 1.14.13.117 isoleucine N-monooxygenase .- 1.14.13.118 valine N-monooxygenase .- 1.14.14.7 tryptophan 7-halogenase.- 1.14.14.8 anthranilate 3-monooxygenase (FAD) .- 1.14.15.8 steroid 15b-monooxygenase.- 1.14.19.4 D8-fatty-acid desaturase .- 1.14.19.5 D11-fatty-acid desaturase.- 1.14.19.6 D12-fatty-acid desaturase .- 1.14.21.7 biflaviolin synthase.- 1.14.99.39 ammonia monooxygenase .- 1.14.99.40 5,6-dimethylbenzimidazole synthase .- 1.17.2.1 nicotinate dehydrogenase (cytochrome).- 1.17.5.2 caffeine dehydrogenase .- 1.17.7.1 (E)-4-hydroxy-3-methylbut-2-enyldiphosphate synthase .- 1.20.4.3 Mycoredoxin.- 1.22.1.1 iodotyrosine deiodinase .Offers concise and complete description of about 5,000 enzymes sufficiently well characterized as well as their application in analytical, synthetic and biotechnology processes, in food industry, and for medicinal treatments This new, second edition reflects considerable progress in enzymology: many of the enzymes have either been newly classified, or re-classified Content in this new 2nd edition has more than doubled: now consists of 39 volumes + supplements, as well as a synonym index Starting in 2009 all newly classified enzymes are treated in the Supplement Volumes Available in print as well as online
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