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| 003 | BD-SySUS | ||
| 005 | 20160413122451.0 | ||
| 007 | cr nn 008mamaa | ||
| 008 | 130402s2013 gw | s |||| 0|eng d | ||
| 020 |
_a9783642362651 _9978-3-642-36265-1 |
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| 024 | 7 |
_a10.1007/978-3-642-36265-1 _2doi |
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| 050 | 4 | _aQH345 | |
| 050 | 4 | _aQD415-436 | |
| 072 | 7 |
_aPSB _2bicssc |
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| 072 | 7 |
_aSCI007000 _2bisacsh |
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| 082 | 0 | 4 |
_a572 _223 |
| 245 | 1 | 0 |
_aClass 1 Oxidoreductases _h[electronic resource] : _bEC 1 / _cedited by Dietmar Schomburg, Ida Schomburg. |
| 250 | _aSecond Edition. | ||
| 264 | 1 |
_aBerlin, Heidelberg : _bSpringer Berlin Heidelberg : _bImprint: Springer, _c2013. |
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| 300 |
_aXIX, 714 p. _bonline resource. |
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| 336 |
_atext _btxt _2rdacontent |
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| 337 |
_acomputer _bc _2rdamedia |
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| 338 |
_aonline resource _bcr _2rdacarrier |
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| 347 |
_atext file _bPDF _2rda |
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| 490 | 1 | _aSpringer Handbook of Enzymes | |
| 505 | 0 | _a1.1.1.295 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 | _aSpringer 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 | _aLife sciences. | |
| 650 | 0 | _aMolecular biology. | |
| 650 | 0 | _aPharmacology. | |
| 650 | 0 | _aBiotechnology. | |
| 650 | 0 |
_aFood _xBiotechnology. |
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| 650 | 0 | _aVeterinary medicine. | |
| 650 | 0 | _aBiochemistry. | |
| 650 | 1 | 4 | _aLife Sciences. |
| 650 | 2 | 4 | _aBiochemistry, general. |
| 650 | 2 | 4 | _aMolecular Medicine. |
| 650 | 2 | 4 | _aPharmacology/Toxicology. |
| 650 | 2 | 4 | _aFood Science. |
| 650 | 2 | 4 | _aBiotechnology. |
| 650 | 2 | 4 | _aVeterinary Medicine. |
| 700 | 1 |
_aSchomburg, Dietmar. _eeditor. |
|
| 700 | 1 |
_aSchomburg, Ida. _eeditor. |
|
| 710 | 2 | _aSpringerLink (Online service) | |
| 773 | 0 | _tSpringer eBooks | |
| 776 | 0 | 8 |
_iPrinted edition: _z9783642362644 |
| 830 | 0 | _aSpringer Handbook of Enzymes | |
| 856 | 4 | 0 | _uhttp://dx.doi.org/10.1007/978-3-642-36265-1 |
| 912 | _aZDB-2-SBL | ||
| 942 |
_2Dewey Decimal Classification _ceBooks |
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| 999 |
_c46766 _d46766 |
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