Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline benzyl alcohol Identifier CHEBI:17987 (CAS: 100-51-6) help_outline Charge 0 Formula C7H8O InChIKeyhelp_outline WVDDGKGOMKODPV-UHFFFAOYSA-N SMILEShelp_outline OCc1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,190 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline benzaldehyde Identifier CHEBI:17169 (CAS: 100-52-7) help_outline Charge 0 Formula C7H6O InChIKeyhelp_outline HUMNYLRZRPPJDN-UHFFFAOYSA-N SMILEShelp_outline O=Cc1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,120 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:64696 | RHEA:64697 | RHEA:64698 | RHEA:64699 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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The catalytic promiscuity of a microbial 7alpha-hydroxysteroid dehydrogenase. Reduction of non-steroidal carbonyl compounds.
Liu Y., Lv T., Ren J., Wang M., Wu Q., Zhu D.
A thermostable 7α-hydroxysteroid dehydrogenase from Bacteroides fragilis ATCC 25285 was found to catalyze the reduction of various benzaldehyde analogues to their corresponding benzyl alcohols. The enzyme activity was dependent upon the substituent on the benzene ring of the substrates. Benzaldehy ... >> More
A thermostable 7α-hydroxysteroid dehydrogenase from Bacteroides fragilis ATCC 25285 was found to catalyze the reduction of various benzaldehyde analogues to their corresponding benzyl alcohols. The enzyme activity was dependent upon the substituent on the benzene ring of the substrates. Benzaldehydes with electron-withdrawing substituent usually showed higher activity than those with electron-donating groups. Furthermore, this enzyme was tolerant to some organic solvents. These results together with previous studies suggested that 7α-hydroxysteroid dehydrogenase from B. fragilis might play multiple functional roles in biosynthesis and metabolism of bile acids, and in the detoxification of xenobiotics containing carbonyl groups in the large intestine. In addition, its broad substrate spectrum offers great potential for finding applications not only in the synthesis of steroidal compounds of pharmaceutical importance, but also for the production of other high-value fine chemicals. << Less
Steroids 76:1136-1140(2011) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.
Tsigos I., Velonia K., Smonou I., Bouriotis V.
An NAD+-dependent alcohol dehydrogenase (ADH) of the Antarctic psychrophile Moraxella sp. TAE123 was purified to homogeneity with an overall yield of 16.7% and further characterized. The native enzyme had an apparent molecular mass of 240 kDa and consisted of four identical 52-kDa subunits. The pI ... >> More
An NAD+-dependent alcohol dehydrogenase (ADH) of the Antarctic psychrophile Moraxella sp. TAE123 was purified to homogeneity with an overall yield of 16.7% and further characterized. The native enzyme had an apparent molecular mass of 240 kDa and consisted of four identical 52-kDa subunits. The pI of the enzyme was determined to be 5.5, while its optimum pH is 7.5. The enzyme contained 1 zinc atom/subunit and exhibited a remarkable thermal lability. Moraxella sp. TAE123 ADH exhibited a wide range of substrate specificity similar to its mammalian counterparts and in contrast to other microbial ADHs. It oxidized mainly primary and secondary aliphatic alcohols. The highest reaction rate was observed when ethanol was used as substrate. A gradual decrease in rate was observed by increasing the length and branching of the carbon chain of the alcohol. This enzyme oxidized effectively large bulky alcohols, such as diphenylmethanol. Reduction of aldehydes and ketones was also observed. N-terminal amino acid sequence analysis of the enzyme did not reveal any similarity with the amino termini of all other ADHs, while an unexpected significant similarity was observed with the amino terminal sequence of four prokaryotic aldehyde dehydrogenases. << Less
Eur. J. Biochem. 254:356-362(1998) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.