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Class 1 Oxidoreductases EC 1 /

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 class...

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Bibliographic Details
Corporate Author: SpringerLink (Online service)
Other Authors: Schomburg, Dietmar. (Editor), Schomburg, Ida. (Editor)
Format: Electronic
Language:English
Published: Berlin, Heidelberg : Springer Berlin Heidelberg : Imprint: Springer, 2013.
Edition:Second Edition.
Series:Springer Handbook of Enzymes
Subjects:
Life sciences.
Medicine.
Toxicology.
Biotechnology.
Food science.
Veterinary medicine.
Biochemistry.
Life Sciences.
Biochemistry, general.
Molecular Medicine.
Pharmacology/Toxicology.
Food Science.
Veterinary Medicine.
Online Access:https://ezaccess.library.uitm.edu.my/login?url=http://dx.doi.org/10.1007/978-3-642-36265-1
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505 0 # |a 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 . 
520 # # |a 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. 
650 # 0 |a Life sciences. 
650 # 0 |a Medicine. 
650 # 0 |a Toxicology. 
650 # 0 |a Biotechnology. 
650 # 0 |a Food science. 
650 # 0 |a Veterinary medicine. 
650 # 0 |a Biochemistry. 
650 1 4 |a Life Sciences. 
650 2 4 |a Biochemistry, general. 
650 2 4 |a Molecular Medicine. 
650 2 4 |a Pharmacology/Toxicology. 
650 2 4 |a Food Science. 
650 2 4 |a Biotechnology. 
650 2 4 |a Veterinary Medicine. 
700 1 # |a Schomburg, Ida.  |e editor. 
710 2 # |a SpringerLink (Online service) 
773 0 # |t Springer eBooks 
776 0 8 |i Printed edition:  |z 9783642362644 
830 # 0 |a Springer Handbook of Enzymes 
856 4 0 |u https://ezaccess.library.uitm.edu.my/login?url=http://dx.doi.org/10.1007/978-3-642-36265-1 
912 # # |a ZDB-2-SBL 
950 # # |a Biomedical and Life Sciences (Springer-11642) 

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