Sulcatone reductase: Difference between revisions
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{{enzyme |
{{infobox enzyme |
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| Name = sulcatone reductase |
| Name = sulcatone reductase |
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| EC_number = 1.1.1.260 |
| EC_number = 1.1.1.260 |
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| CAS_number = 196522-54-0 |
| CAS_number = 196522-54-0 |
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| GO_code = 0050491 |
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| IUBMB_EC_number = 1/1/1/260 |
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In [[enzymology]], a '''sulcatone reductase''' ({{EC number|1.1.1.260}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
In [[enzymology]], a '''sulcatone reductase''' ({{EC number|1.1.1.260}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
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Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[sulcatol]] and [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[sulcatone]], [[nicotinamide adenine dinucleotide|NADH]], and [[hydrogen ion|H<sup>+</sup>]]. |
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[sulcatol]] and [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[sulcatone]], [[nicotinamide adenine dinucleotide|NADH]], and [[hydrogen ion|H<sup>+</sup>]]. |
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This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. |
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor. The [[List of enzymes|systematic name]] of this enzyme class is '''sulcatol:NAD<sup>+</sup> oxidoreductase'''. |
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==References== |
==References== |
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{{reflist|1}} |
{{reflist|1}} |
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* {{cite journal | |
* {{cite journal | vauthors = Belan A, Botle J, Fauve A, Gourcy JG, Veschambre H | date = 1987 | title = Use of biological systems for the preparation of chiral molecules 3. An application in pheromone synthesis: Preparation of sulcatol enantiomers | journal = J. Org. Chem. | volume = 52 | pages = 256–260 | doi = 10.1021/jo00378a017 | issue = 2 }} |
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* {{cite journal | |
* {{cite journal | vauthors = Tidswell EC, Salter GJ, Kell DB, Morris JG | date = 1997 | title = Enantioselectivity of sulcatone reduction by some anaerobic bacteria | journal = Enzyme and Microbial Technology | volume = 21 | pages = 143–147 | doi = 10.1016/S0141-0229(96)00264-5 | issue = 2 }} |
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* {{cite journal | |
* {{cite journal | vauthors = Tidswell EC, Thompson AN, Morris JG | date = 1991 | title = Selection in chemostat culture of a mutant strain of ''Clostridium tryobutyricum'' improved in its reduction of ketones | journal = J. Appl. Microbiol. Biotechnol. | volume = 35 | pages = 317–322 }} |
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{{Alcohol oxidoreductases}} |
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{{Enzymes}} |
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{{Portal bar|Biology|border=no}} |
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[[Category:EC 1.1.1]] |
[[Category:EC 1.1.1]] |
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[[Category:NADH-dependent enzymes]] |
[[Category:NADH-dependent enzymes]] |
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[[Category:Enzymes of unknown structure]] |
[[Category:Enzymes of unknown structure]] |
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Latest revision as of 15:56, 26 August 2023
| sulcatone reductase | |||||||||
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| Identifiers | |||||||||
| EC no. | 1.1.1.260 | ||||||||
| CAS no. | 196522-54-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a sulcatone reductase (EC 1.1.1.260) is an enzyme that catalyzes the chemical reaction
- sulcatol + NAD+ sulcatone + NADH + H+
Thus, the two substrates of this enzyme are sulcatol and NAD+, whereas its 3 products are sulcatone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sulcatol:NAD+ oxidoreductase.
References
[edit]- Belan A, Botle J, Fauve A, Gourcy JG, Veschambre H (1987). "Use of biological systems for the preparation of chiral molecules 3. An application in pheromone synthesis: Preparation of sulcatol enantiomers". J. Org. Chem. 52 (2): 256–260. doi:10.1021/jo00378a017.
- Tidswell EC, Salter GJ, Kell DB, Morris JG (1997). "Enantioselectivity of sulcatone reduction by some anaerobic bacteria". Enzyme and Microbial Technology. 21 (2): 143–147. doi:10.1016/S0141-0229(96)00264-5.
- Tidswell EC, Thompson AN, Morris JG (1991). "Selection in chemostat culture of a mutant strain of Clostridium tryobutyricum improved in its reduction of ketones". J. Appl. Microbiol. Biotechnol. 35: 317–322.
