2.3.1.84: alcohol O-acetyltransferase
This is an abbreviated version!
For detailed information about alcohol O-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.84
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2.3.1.84
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isoamyl
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sake
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fruity
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kyokai
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tatase
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2-phenylethyl
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uvarum
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wickerhamomyces
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l-asp
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self-cloning
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synthesis
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hanseniaspora
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acetate-producing
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brewery
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biotechnology
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nutrition
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analysis
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food industry
- 2.3.1.84
-
isoamyl
-
sake
- fruity
-
kyokai
- tatase
-
2-phenylethyl
- uvarum
-
wickerhamomyces
- l-asp
-
self-cloning
- synthesis
- hanseniaspora
-
acetate-producing
-
brewery
- biotechnology
- nutrition
- analysis
- food industry
Reaction
Synonyms
AAT, AAT1, Aat2, AATase, AATFase, acetyltransferase, alcohol, AFT1, AFT2, alcohol acetyl transferase Atf1p, alcohol acetyl transferase I, alcohol acetyl-transferase, alcohol acetyl-transferase 1, alcohol acetyl-transferase 2, alcohol acetyltransferase, alcohol acetyltransferase AFT1, alcohol acetyltransferase AFT2, alcohol acetyltransferase ATF1, alcohol acetyltransferase ATF2, alcohol acetyltransferase I, alcohol acetyltransferase Lg-ATF1, ATF1, ATF1-encoded alcohol acetyltransferases, ATF2, ATF2-encoded alcohol acetyltransferases, CFAT1, CFAT2, coniferyl alcohol acetyltransferase, GAAT, geraniol AAT, geraniol:acetyl CoA acetyltransferase, geraniol:acetyl coenzyme A acetyltransferase, KlAtf, Lg-ATF1, PhCFAT, RhAAT
ECTree
2.3.1.84 alcohol O-acetyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.84 - alcohol O-acetyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E509A/E512A/E513A
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mutation in isoform Atf1, mutated protein shows 84% localization to lipid droplets
L511A/L514A/Y518A/L512A
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mutation in isoform Atf1, loss of membrane association
R22A/R23A/R36A
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mutation in isoform Atf2, protein is localized in the cytoplasm
W518A/F521/I529A/F532A R36A
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mutation in isoform Atf2, protein is localized in the cytoplasm
E509A/E512A/E513A
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mutation in isoform Atf1, mutated protein shows 84% localization to lipid droplets
-
L511A/L514A/Y518A/L512A
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mutation in isoform Atf1, loss of membrane association
-
R22A/R23A/R36A
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mutation in isoform Atf2, protein is localized in the cytoplasm
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W518A/F521/I529A/F532A R36A
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mutation in isoform Atf2, protein is localized in the cytoplasm
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additional information
additional information
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truncation of amphipathic helices within the N- and C-terminal domains of isoform Atf1 (residues 24-41 and 508-525) impair endoplasmic reticulum localization and membrane association. Mutations of the basic or hydrophobic residues in the N-terminal helix and hydrophobic residues in the C-terminal helix of Atf1 disrupt ER association and subsequent sorting from the ER to lipid droplets. Similar amphipathic helices are found at both ends of isoform Atf2, enabling ER and lipid droplet association. Mutations to the N- and C-terminal helices of Atf2 prevent membrane association
additional information
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reconstruction of the engineered pathways for production of indole-3-ethanol and indole-3-ethanol acetate from glucose in Escherichia coli strain MG1655, enzyme ATF1 is included catalyzing the formation of indole-3-ethanol acetate from indole-3-ethanol, pathway and method evaluation, overview
additional information
-
truncation of amphipathic helices within the N- and C-terminal domains of isoform Atf1 (residues 24-41 and 508-525) impair endoplasmic reticulum localization and membrane association. Mutations of the basic or hydrophobic residues in the N-terminal helix and hydrophobic residues in the C-terminal helix of Atf1 disrupt ER association and subsequent sorting from the ER to lipid droplets. Similar amphipathic helices are found at both ends of isoform Atf2, enabling ER and lipid droplet association. Mutations to the N- and C-terminal helices of Atf2 prevent membrane association
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additional information
-
reconstruction of the engineered pathways for production of indole-3-ethanol and indole-3-ethanol acetate from glucose in Escherichia coli strain MG1655, enzyme ATF1 is included catalyzing the formation of indole-3-ethanol acetate from indole-3-ethanol, pathway and method evaluation, overview
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