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 … Plus…
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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 Frais d'envoizzgl. Versandkosten., Livraison non-comprise 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 … Plus…
ISBN: 9783642362651
Life Sciences; Biochemistry, general; Molecular Medicine; Pharmacology/Toxicology; Food Science; Biotechnology; Veterinary Medicine/Veterinary Science Applied Microbiology, Biochemistry, … Plus…
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]
Données bibliographiques du meilleur livre correspondant
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Informations détaillées sur le livre - Class 1 Oxidoreductases
EAN (ISBN-13): 9783642362651
ISBN (ISBN-10): 3642362656
Date de parution: 2013
Editeur: Springer-Verlag
714 Pages
Langue: eng/Englisch
Livre dans la base de données depuis 2012-07-14T08:49:40+02:00 (Zurich)
Page de détail modifiée en dernier sur 2024-01-19T07:06:34+01:00 (Zurich)
ISBN/EAN: 3642362656
ISBN - Autres types d'écriture:
3-642-36265-6, 978-3-642-36265-1
Autres types d'écriture et termes associés:
Auteur du livre: chang, chan, antje, schomburg, schöm
Titre du livre: cla, class
Données de l'éditeur
Auteur: Dietmar Schomburg; Ida Schomburg; Antje Chang
Titre: Springer Handbook of Enzymes; Class 1 Oxidoreductases - EC 1
Editeur: Springer; Springer Berlin
714 Pages
Date de parution: 2013-04-01
Berlin; Heidelberg; DE
Langue: Anglais
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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