Enzymes
| UniProtKB help_outline | 4 proteins |
| Enzyme class help_outline |
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| GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline acetyl-CoA Identifier CHEBI:57288 (Beilstein: 8468140) help_outline Charge -4 Formula C23H34N7O17P3S InChIKeyhelp_outline ZSLZBFCDCINBPY-ZSJPKINUSA-J SMILEShelp_outline CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 352 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an aliphatic alcohol Identifier CHEBI:2571 Charge 0 Formula HOR SMILEShelp_outline O* 2D coordinates Mol file for the small molecule Search links Involved in 214 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an acetyl ester Identifier CHEBI:47622 Charge 0 Formula C2H3O2R SMILEShelp_outline CC(=O)O[*] 2D coordinates Mol file for the small molecule Search links Involved in 106 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,500 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:17229 | RHEA:17230 | RHEA:17231 | RHEA:17232 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
- RHEA:65468
- RHEA:65460
- RHEA:65456
- RHEA:65236
- RHEA:64676
- RHEA:64632
- RHEA:64628
- RHEA:64624
- RHEA:55972
- RHEA:28254
Publications
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The purification, properties and internal peptide sequences of alcohol acetyltransferase isolated from Saccharomyces cerevisiae Kyokai No. 7.
Minetoki T., Bogaki T., Iwamatsu A., Fujii T., Hamachi M.
Alcohol acetyltransferase (AATase) catalyzes the esterification of isoamyl alcohol by acetyl coenzyme A. The enzyme was solubilized from the microsomal fraction of Saccharomyces cerevisiae Kyokai No. 7, using Triton X-100 and then purified by a series of chromatographic separations: Poly Buffer Ex ... >> More
Alcohol acetyltransferase (AATase) catalyzes the esterification of isoamyl alcohol by acetyl coenzyme A. The enzyme was solubilized from the microsomal fraction of Saccharomyces cerevisiae Kyokai No. 7, using Triton X-100 and then purified by a series of chromatographic separations: Poly Buffer Exchanger 94 (PBE94), DEAE Toyopearl, Toyopearl HW60, hydroxyapatite, Octyl-Sepharose CL-4B, and hexanol-affinity column chromatography. When the solubilized enzyme was put on PBE94, two active fractions were obtained. The enzyme obtained after affinity column chromatography had a single band on an SDS polyacrylamide gel, and its molecular mass was estimated to be 60 kDa. The enzyme was most active at pH 8.0 and 25 degrees C. It was stable between pH 7.5 and 8.5, but was unstable at temperatures above 10 degrees C. The activity was markedly inhibited by heavy metal ions such as Cd2+, Cu2+, Zn2+, and Hg2+, and sulfhydryl reagents. The Km for acetyl-CoA was 0.19 mM. The internal peptide sequences were also identified. << Less
Biosci. Biotechnol. Biochem. 57:2094-2098(1993) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
Comments
Published in "Ester formation by alcohol acetyltransferase from brewers' yeast." Yoshioka, K. and Hashimoto, N. Agric. Biol. Chem. 45 (1981) 2183–2190.