2.3.1.31: homoserine O-acetyltransferase
This is an abbreviated version!
For detailed information about homoserine O-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.31
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2.3.1.31
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l-methionine
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ping-pong
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o-acetylhomoserine
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acetyl-enzyme
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succinyl-coa
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sulfhydrylase
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gamma-hydroxyl
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o-acetyl-l-homoserine
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medicine
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molecular biology
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drug development
- 2.3.1.31
- l-methionine
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ping-pong
- o-acetylhomoserine
-
acetyl-enzyme
- succinyl-coa
-
sulfhydrylase
-
gamma-hydroxyl
- o-acetyl-l-homoserine
- medicine
- molecular biology
- drug development
Reaction
Synonyms
acetyltransferase, homoserine, CnHTA, DcsE, HAT, homoserine acetyltransferase, homoserine O-acetyltransferase, homoserine transacetylase, homoserine transsuccinylase, homoserine-O-transacetylase, HTA, HTS, L-homoserine O-acetyltransferase, MaHTA, MaMetX, MET2, MetA, MetX, MetXA, metX_1, metX_2, MhHTA, MhMetX, MsHAT, MtHTA, MtMetX, TmHTS
ECTree
2.3.1.31 homoserine O-acetyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.31 - homoserine O-acetyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C142A
C142S
E111G
E237A
E237D
E237Q
E250A
H235A
H235N
H235Q
K163M
K47M
K47R
R249M
S192A
S143A
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mutant does not show any acetyltransferase activity. Incubation of mutant HTAH with ebelactone A and inhibitor does not generate an enzyme-inhibitor adduct
D315A
site-directed mutagenesis, the mutant shows an almost complete loss of activity
H345A
site-directed mutagenesis, the mutant shows an almost complete loss of activity
K267A
site-directed mutagenesis, the mutant shows a slight loss in activity
L55A
site-directed mutagenesis, the mutant shows a slight loss in activity
Q244A
site-directed mutagenesis, the mutant shows a slight loss in activity
R238A
site-directed mutagenesis, the mutant shows a slight loss in activity
S152A
site-directed mutagenesis, the mutant shows an almost complete loss of activity
S259A
site-directed mutagenesis, the mutant shows a slight loss in activity
T56A
site-directed mutagenesis, the mutant shows a slight loss in activity
Y263A
site-directed mutagenesis, the mutant shows a slight loss in activity
H345A
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site-directed mutagenesis, the mutant shows an almost complete loss of activity
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K267A
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site-directed mutagenesis, the mutant shows a slight loss in activity
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R238A
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site-directed mutagenesis, the mutant shows a slight loss in activity
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S152A
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site-directed mutagenesis, the mutant shows an almost complete loss of activity
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T56A
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site-directed mutagenesis, the mutant shows a slight loss in activity
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D209N
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kcat/Km for acetyl-CoA is 1.45fold lower than wild-type value, kcat/Km for L-homocysteine is 1.6fold higher than wild-type value
D374N
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kcat/Km for acetyl-CoA is 1.6fold than wild-type value, kcat/Km for L-homocysteine is 1.6fold higher than wild-type value
S163C
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kcat/Km for acetyl-CoA is 16.7fold than wild-type value, kcat/Km for L-homocysteine is 33fold lower than wild-type value
G52A
site-directed mutagenesis, no activity with L-serine, but with L-homoserine, although the mutant is less active than the wild-type enzyme
G52A/P55G
site-directed mutagenesis, no activity with L-serine, but with L-homoserine, activity with L-homoserine is increased compared to the wild-type enzyme
P55G
site-directed mutagenesis, increased activity with L-serine and with L-homoserine compared to the wild-type enzyme
G52A
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site-directed mutagenesis, no activity with L-serine, but with L-homoserine, although the mutant is less active than the wild-type enzyme
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P55G
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site-directed mutagenesis, increased activity with L-serine and with L-homoserine compared to the wild-type enzyme
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additional information
E111G
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mutant protein shows no detectable activity with acetyl-CoA but catalyzes an acyltransferase reaction using succinyl-CoA and homoserine (kcat (succinyl-CoA): 0.8/sec, Km (succinyl-CoA): 0.273 mM, Km (L-homoserine): 0.2 mM)
E111G
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no activity with acetyl-CoA, but with succinyl-CoA and homoserine, glutamic acid 111 (corresponding to Escherichia coli residue with function in succinyl-specificity of homoserine transsuccinylase) sterically occludes fitting of a succinyl-enzyme intermediate in the active site
E237A
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compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
E237D
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compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
E237Q
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compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
E250A
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compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
E250A
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13-14fold increase in homoserine Km value, homoserine binding is affected not acetyl-CoA binding
K163M
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compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
K163M
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13-14fold increase in homoserine Km value, homoserine binding is affected not acetyl-CoA binding
K47M
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compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
K47M
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turnover number is reduced 14fold, Km value for acetyl-CoA is reduced 17fold, function in acetyl-CoA binding
K47R
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compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
R249M
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compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
R249M
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10fold reduction in kcat, 64fold higher Km for homoserine than wild-type, homoserine binding is affected not acetyl-CoA binding
S192A
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compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
S192A
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5fold increase in Km for homoserine, homoserine binding is affected not acetyl-CoA binding
additional information
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Met auxotrophy is shown by a constructed MET2 mutant and its growth behavior in Met-deficient media
additional information
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construction of the methionine auxotroph mutant strain Z43R3912 by restriction enzyme-mediated integration REMI, the mutant strain shows pleiotrophic phenotypes including reduced virulence on host cereal plants and lack of sexual development, overview, mutation is tagged with the hygromycin B resistance marker and insertion can be located in the HOA gene ancoding the enzyme, complementation of the mutants methionine auxotrophy by expression of metE and GrzmetE genes from Aspergillus nidulans
additional information
construction of truncated enzyme and isolated active site
additional information
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construction of truncated enzyme and isolated active site
additional information
construction of truncated enzyme and isolated active site
additional information
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construction of truncated enzyme and isolated active site
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additional information
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construction of truncated enzyme and isolated active site
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additional information
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construction of truncated enzyme and isolated active site
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additional information
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construction of truncated enzyme and isolated active site
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additional information
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construction of truncated enzyme and isolated active site
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additional information
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construction of truncated enzyme and isolated active site
-
additional information
construction of truncated enzyme and isolated active site
additional information
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construction of truncated enzyme and isolated active site
additional information
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construction of truncated enzyme and isolated active site
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additional information
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construction of truncated enzyme and isolated active site
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additional information
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construction of truncated enzyme and isolated active site
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additional information
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construction of truncated enzyme and isolated active site
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additional information
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methionine deficient strains do not perform the L-homoserine/O-acetyl-L-homoserine exchange reaction
additional information
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methionine auxotroph strains show no activity
additional information
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methionine auxotroph strains show no activity
