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EC Tree
IUBMB Comments The enzyme, characterized from the yeast Saccharomyces cerevisiae, hydrolyses acetate esters. It acts preferentially on 3-methylbutyl acetate, a major determinant of sake flavor.
The enzyme appears in viruses and cellular organisms
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IAH1
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3-methylbutyl acetate + H2O = 3-methylbutanol + acetate
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3-methylbutyl acetate acetohydrolase
The enzyme, characterized from the yeast Saccharomyces cerevisiae, hydrolyses acetate esters. It acts preferentially on 3-methylbutyl acetate, a major determinant of sake flavor.
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2-methylpropyl acetate + H2O
2-methylpropanol + acetate
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?
3-methylbutyl acetate + H2O
3-methylbutanol + acetate
about 80% of the activity with 2-methylpropyl acetate
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?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
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?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
very poor substrate
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?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
poor substrate
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?
isopropyl acetate + H2O
isopropanol + acetate
about 70% of the activity with 2-methylpropyl acetate
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?
N-propyl acetate + H2O
n-propanol + acetate
about 85% of the activity with 2-methylpropyl acetate
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4-chloromercuribenzoate
0.1 mM, 40% residual activity
diisopropyl fluorophosphate
0.1 mM, no residual activity
Hg2+
1 mM, no residual activity
iodoacetamide
1 mM, no residual activity
Triton X-100
1%, 72% residual activtiy
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2-mercaptoethanol
1 mM, 143% of initial activity
dithiothreitol
1 mM, 160% of initial activity
EDTA
1 mM, 133% of initial activity
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15.3
2-methylpropyl acetate
pH 7.0, 25°C
40.3
3-methylbutyl acetate
pH 7.0, 25°C
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UniProt
brenda
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IAH1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
238
0
27346
Swiss-Prot
-
IAH1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
246
0
27991
Swiss-Prot
other Location (Reliability: 3 )
A0A6J8ASH4_MYTCO
237
0
26566
TrEMBL
-
A0A6J8ARY3_MYTCO
235
0
26388
TrEMBL
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?
x * 28000, SDS-PAGE, x * 37305, calculated from sequence
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to 1.6 A resolution, space group P21, with unit-cell parameters a 71.5 A, b 44.6 A, c 81.8 A, and beta 114.4°
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expression in Escherichia coli
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food industry
balance of enzyme activities of alcohol acetyltransferase AATFase and isoamyl acetate esterase Iah1 is important for optimum production of isoamyl acetate in sake brewing. The amount of isoamyl acetate in the sake increases with an increasing ratio of AATFase/Iah1 esterase activity
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Fukuda, K.; Yamamoto, N.; Kiyokawa, Y.; Yanagiuchi, T.; Wakai, Y.; Kitamoto, K.; Inoue, Y.; Kimura, A.
Balance of activities of alcohol acetyltransferase and esterase in Saccharomyces cerevisiae is important for production of isoamyl acetate
Appl. Environ. Microbiol.
64
4076-4078
1998
Saccharomyces cerevisiae (P41734)
brenda
Fukuda, K.; Kiyokawa, Y.; Yanagiuchi, T.; Wakai, Y.; Kitamoto, K.; Inoue, Y.; Kimura, A.
Purification and characterization of isoamyl acetate-hydrolyzing esterase encoded by the IAH1 gene of Saccharomyces cerevisiae from a recombinant Escherichia coli
Appl. Microbiol. Biotechnol.
53
596-600
2000
Saccharomyces cerevisiae (P41734)
brenda
Ma, J.; Lu, Q.; Yuan, Y.; Ge, H.; Li, K.; Zhao, W.; Gao, Y.; Niu, L.; Teng, M.
Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae reveals a novel active site architecture and the basis of substrate specificity
Proteins
79
662-668
2011
Saccharomyces cerevisiae (P41734)
brenda
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Enzyme Nomenclature
3.1.1.112 isoamyl acetate esteras
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