Enzymes
| UniProtKB help_outline | 3 proteins |
| Enzyme class help_outline |
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- Name help_outline (E)-cinnamyl alcohol Identifier CHEBI:33227 (Beilstein: 741973; CAS: 104-54-1,4407-36-7) help_outline Charge 0 Formula C9H10O InChIKeyhelp_outline OOCCDEMITAIZTP-QPJJXVBHSA-N SMILEShelp_outline OC\C=C\c1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- 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 321 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (E)-cinnamyl acetate Identifier CHEBI:156069 Charge 0 Formula C11H12O2 InChIKeyhelp_outline WJSDHUCWMSHDCR-VMPITWQZSA-N SMILEShelp_outline C1=CC(=CC=C1)/C=C/COC(C)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 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 1,468 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:36151 | RHEA:36152 | RHEA:36153 | RHEA:36154 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Characterization of a petunia acetyltransferase involved in the biosynthesis of the floral volatile isoeugenol.
Dexter R., Qualley A., Kish C.M., Ma C.J., Koeduka T., Nagegowda D.A., Dudareva N., Pichersky E., Clark D.
Petunia flower petals emit large amounts of isoeugenol, which has been shown to be synthesized by isoeugenol synthase (PhIGS1) from an ester of coniferyl alcohol, hypothesized to be coniferyl acetate. This paper describes the identification and characterization of a novel petunia gene encoding an ... >> More
Petunia flower petals emit large amounts of isoeugenol, which has been shown to be synthesized by isoeugenol synthase (PhIGS1) from an ester of coniferyl alcohol, hypothesized to be coniferyl acetate. This paper describes the identification and characterization of a novel petunia gene encoding an enzyme belonging to the BAHD acyltransferase family whose expression correlates with isoeugenol biosynthesis. RNAi suppression of this gene results in inhibition of isoeugenol biosynthesis. Biochemical characterization of the protein encoded by this gene showed that it has acetyltransferase activity and is most efficient with coniferyl alcohol among the alcohol substrates tested. Overall, these data support the conclusion that coniferyl acetate is the substrate of isoeugenol synthase. << Less
Plant J. 49:265-275(2007) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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Characterization of benzylalcohol acetyltransferases in scented and non-scented Clarkia species.
Nam K.H., Dudareva N., Pichersky E.
The floral scent of Clarkia breweri, an annual native to California, contains copious amounts of benzylacetate, which is synthesized by a reaction of benzylalcohol and acetyl-CoA that is catalyzed by acetyl-CoA:benzylalcohol acetyltransferase (BEAT). Here we demonstrate that different lines of C. ... >> More
The floral scent of Clarkia breweri, an annual native to California, contains copious amounts of benzylacetate, which is synthesized by a reaction of benzylalcohol and acetyl-CoA that is catalyzed by acetyl-CoA:benzylalcohol acetyltransferase (BEAT). Here we demonstrate that different lines of C. breweri contain different levels of BEAT activity even though they have similar levels of BEAT mRNA. We also present evidence that the genome of C. breweri's non-scented progenitor, C. concinna, contains BEAT genes, but that its flowers have little BEAT enzymatic activity. This is due to the fact that although C. concinna BEAT genes are transcribed in the flowers, the single intron in these transcripts is almost never spliced out, and when the intron is spliced out, the resulting enzyme has higher affinity with substrates other than benzylalcohol. These results indicate that the regulation of BEAT activity in Clarkia involves post-transcriptional mechanisms. << Less
Plant Cell Physiol. 40:916-923(1999) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Acetyl-CoA:benzylalcohol acetyltransferase--an enzyme involved in floral scent production in Clarkia breweri.
Dudareva N., D'Auria J.C., Nam K.H., Raguso R.A., Pichersky E.
Volatile esters impart distinct characteristics to the floral scent of many plants, and are important in attracting insect pollinators. They are also important flavor compounds in fruits. The ester benzylacetate is a major constituent of the floral scent of Clarkia breweri, an annual plant native ... >> More
Volatile esters impart distinct characteristics to the floral scent of many plants, and are important in attracting insect pollinators. They are also important flavor compounds in fruits. The ester benzylacetate is a major constituent of the floral scent of Clarkia breweri, an annual plant native to California. The enzyme acetyl-CoA:benzylalcohol acetyltransferase (BEAT), which catalyzes the formation of benzylacetate, has been purified from C. breweri petals, and a cDNA encoding this enzyme has been isolated and characterized. The sequence of the 433-residue BEAT protein does not show high similarity to any previously characterized protein, but a 35-residue region from position 135-163 has significant similarity (42-56% identity) to several proteins known or suspected to use an acyl-CoA substrate. E. coli cells expressing C. breweri BEAT produced enzymatically active protein, and also synthesized benzylacetate and secreted it into the medium. Of the different parts of the C. breweri flower, petals contained the majority of BEAT transcripts, and no BEAT mRNA was detected in leaves. The levels of BEAT mRNA in the petals increased as the bud matured, and peaked at anthesis, paralleling changes in BEAT activity. However, three days after anthesis, mRNA levels began a steep decline, whereas BEAT activity remained high for the next two days, suggesting that the BEAT protein is relatively stable. << Less
Plant J. 14:297-304(1998) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.