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acetyl-CoA + 3-amino-1-propanol
?
-
low activity
-
-
r
acetyl-CoA + 4-nitrophenyl acetate
?
-
low activity
-
-
r
acetyl-CoA + D-homoserine
CoA + O-acetyl-D-homoserine
acetyl-CoA + gamma-hydroxybutyric acid
?
-
-
-
-
r
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
beta-hydroxybutyryl-CoA + L-homoserine
CoA + beta-hydroxybutyryl-L-homoserine
-
-
-
-
?
butyryl-CoA + L-homoserine
CoA + O-butyryl-L-homoserine
crotonyl-CoA + L-homoserine
CoA + O-crotonyl-L-homoserine
-
low activity
-
-
r
glutaryl-CoA + L-homoserine
CoA + O-glutaryl-L-homoserine
isobutyryl-CoA + L-homoserine
CoA + O-isobutyryl-L-homoserine
-
-
-
-
?
malonyl-CoA + L-homoserine
CoA + O-malonyl-L-homoserine
-
-
-
-
?
propionyl-CoA + L-homoserine
CoA + O-propionyl-L-homoserine
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
additional information
?
-
acetyl-CoA + D-homoserine
CoA + O-acetyl-D-homoserine
-
-
-
-
r
acetyl-CoA + D-homoserine
CoA + O-acetyl-D-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
functions as homoserine transacetylase rather than homoserine transsuccinylase despite its more than 50% sequence identity with homoserine transsuccinylase
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
preference for acetyl-CoA
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
first reaction in L-methionine biosynthesis
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
a key enzyme in methionine biosynthesis
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
preference for acetyl-CoA
-
r
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
control point in the pathway
-
r
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
first reaction in L-methionine biosynthesis
-
r
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
first reaction in L-methionine biosynthesis
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
intermediate in methionine biosynthesis
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
acetyl imidazole cannot replace acetyl-CoA
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
acetyl phosphate, acetyl carnitine, acetyl-[acyl-carrier-protein] from E. coli
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
acetyl phosphate, acetyl carnitine, acetyl-[acyl-carrier-protein] from E. coli
-
ir
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
succinyl-CoA cannot replace acetyl-CoA
-
ir
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
not D-homoserine or any other hydroxy-L-amino acid
-
ir
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
the enzyme is a catalyst in the biochemical pathway that metabolizes Asp to Met in fungi
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
homoserine transacetylase catalyzes the acetylation of L-homoserine via a covalent acyl-enzyme intermediate through an active-site Ser
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
the enzyme utilizes a ping-pong kinetic mechanism in which the acetate group of acetyl-CoA is initially transferred to an enzyme nucleophile before subsequent transfer to homoserine
-
-
r
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
-
-
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
succinyl-CoA cannot replace acetyl-CoA
-
?
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
-
first reaction in L-methionine biosynthesis
-
-
?
butyryl-CoA + L-homoserine
CoA + O-butyryl-L-homoserine
-
-
-
-
?
butyryl-CoA + L-homoserine
CoA + O-butyryl-L-homoserine
-
-
-
-
?
glutaryl-CoA + L-homoserine
CoA + O-glutaryl-L-homoserine
-
very low activity
-
-
r
glutaryl-CoA + L-homoserine
CoA + O-glutaryl-L-homoserine
-
-
-
-
?
propionyl-CoA + L-homoserine
CoA + O-propionyl-L-homoserine
-
-
-
-
?
propionyl-CoA + L-homoserine
CoA + O-propionyl-L-homoserine
-
-
-
-
?
propionyl-CoA + L-homoserine
CoA + O-propionyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
activity of mutant E111G
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
very low activity
-
-
r
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
additional information
?
-
-
catalyzes reversible L-homoserine/O-acetyl-L-homoserine exchange in the absence of acetyl-CoA
-
-
?
additional information
?
-
-
catalyzes reversible L-homoserine/O-acetyl-L-homoserine exchange in the absence of acetyl-CoA
-
-
?
additional information
?
-
-
catalyzes reversible L-homoserine/O-acetyl-L-homoserine exchange in the absence of acetyl-CoA
-
-
?
additional information
?
-
-
deacylates acetyl-CoA in the absence of L-homoserine
-
-
?
additional information
?
-
-
catalyzes reversible L-homoserine/O-acetyl-L-homoserine exchange in the absence of acetyl-CoA
-
-
?
additional information
?
-
the enzyme prefers L-serine as a substrate, cf. EC 2.3.1.30, but is also active with L-homoserine, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme prefers L-serine as a substrate, cf. EC 2.3.1.30, but is also active with L-homoserine, substrate specificity, overview
-
-
?
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71
3-Amino-1-propanol
-
-
19
4-hydroxybutyric acid
-
-
1.4
4-nitrophenyl acetate
-
-
0.083
beta-hydroxybutyryl-CoA
-
25°C, pH 7.5
0.0441 - 0.21
butyryl-CoA
0.068
isobutyryl-CoA
-
25°C, pH 7.5
0.017
malonyl-CoA
-
25°C, pH 7.5
0.85
O-acetyl-L-homoserine
-
-
1.7
O-acetylhomoserine
-
25°C, pH 7.5
0.044 - 0.09
propionyl-CoA
0.051 - 0.36
succinyl-CoA
additional information
additional information
-
0.0116
acetyl-CoA
-
21°C, pH 8.0, mutant enzyme
0.012
acetyl-CoA
-
deacylation
0.0199
acetyl-CoA
-
21°C, pH 8.0, mutant enzyme
0.0209
acetyl-CoA
-
21°C, pH 8.0, wild-type enzyme
0.0239
acetyl-CoA
-
21°C, pH 8.0, mutant enzyme
0.108
acetyl-CoA
-
mutant E237A
0.108
acetyl-CoA
-
E237A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.13
acetyl-CoA
-
25°C, pH 7.5
0.143
acetyl-CoA
-
mutant E237Q
0.143
acetyl-CoA
-
E237Q, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.158
acetyl-CoA
recombinant His-tagged enzyme, pH 8.0, 22°C
0.165
acetyl-CoA
-
mutant E250A
0.165
acetyl-CoA
-
E250A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.174
acetyl-CoA
-
mutant E237D
0.174
acetyl-CoA
-
E237D, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.185
acetyl-CoA
-
wild-type
0.185
acetyl-CoA
-
wild-type, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.199
acetyl-CoA
-
mutant R249M
0.199
acetyl-CoA
-
R249M , 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.249
acetyl-CoA
-
mutant S192A
0.249
acetyl-CoA
-
S192A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.266
acetyl-CoA
-
mutant K163M
0.266
acetyl-CoA
-
K163M, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
1.35
acetyl-CoA
-
mutant K47R
1.35
acetyl-CoA
-
K47R, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
3.07
acetyl-CoA
-
mutant K47M
3.07
acetyl-CoA
-
K47M, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.0441
butyryl-CoA
-
21°C, pH 8.0, wild-type enzyme
0.14
CoA
-
25°C, pH 7.5
4.7
D-homoserine
-
-
280
D-homoserine
-
25°C, pH 7.5
0.18
glutaryl-CoA
-
25°C, pH 7.5
0.06
L-homoserine
recombinant His-tagged enzyme, pH 8.0, 22°C
0.2
L-homoserine
-
E111G, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM succinyl-CoA, 25°C
0.214
L-homoserine
-
wild-type
0.214
L-homoserine
-
wild-type, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.24
L-homoserine
-
25°C, pH 7.5
0.287
L-homoserine
-
mutant E237Q
0.287
L-homoserine
-
E237Q, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.405
L-homoserine
-
mutant E237D
0.405
L-homoserine
-
E237D, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.85
L-homoserine
-
mutant E237A
0.85
L-homoserine
-
E237A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.946
L-homoserine
-
mutant K47R
0.946
L-homoserine
-
K47R, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.96
L-homoserine
-
21°C, pH 8.0, mutant enzyme
1
L-homoserine
recombinant His-tagged mutant P55G enzyme, pH 8.0, 30°C
1.02
L-homoserine
-
mutant S192A
1.02
L-homoserine
-
S192A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
1.09
L-homoserine
-
21°C, pH 8.0, wild-type enzyme
1.15
L-homoserine
-
21°C, pH 8.0, mutant enzyme
1.38
L-homoserine
-
mutant K47M
1.38
L-homoserine
-
K47M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
2
L-homoserine
recombinant His-tagged mutant G52A/P55G enzyme, pH 8.0, 30°C
2.78
L-homoserine
-
mutant K163M
2.78
L-homoserine
-
K163M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
2.95
L-homoserine
-
mutant E250A
2.95
L-homoserine
-
E250A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
6.43
L-homoserine
-
21°C, pH 8.0, mutant enzyme
10
L-homoserine
-
exchange reaction
13.8
L-homoserine
-
mutant R249M
13.8
L-homoserine
-
R249M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
25
L-homoserine
recombinant His-tagged mutant G52A enzyme, pH 8.0, 30°C
98
L-homoserine
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
0.044
propionyl-CoA
-
25°C, pH 7.5
0.0484
propionyl-CoA
-
21°C, pH 8.0, wild-type enzyme
0.051
succinyl-CoA
-
25°C, pH 7.5
0.273
succinyl-CoA
-
E111G, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
additional information
additional information
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
additional information
additional information
-
kcat/Km (substrate L-homoserine): 130000/Msec, (substrate acetyl-CoA): 878000/Msec
-
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0.0074 - 4.56
L-homoserine
2.94
succinyl-CoA
-
E111G, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.0228
acetyl-CoA
-
K47M, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.139
acetyl-CoA
-
E237A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.361
acetyl-CoA
-
E237Q, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.485
acetyl-CoA
-
K47R, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.511
acetyl-CoA
-
R249M , 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.91
acetyl-CoA
-
E237D, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
1.23
acetyl-CoA
-
K163M, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
2.18
acetyl-CoA
-
S192A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
2.64
acetyl-CoA
-
E250A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
5.28
acetyl-CoA
-
wild-type, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C
0.0074
L-homoserine
-
R249M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.009
L-homoserine
recombinant His-tagged mutant G52A enzyme, pH 8.0, 30°C
0.015
L-homoserine
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
0.0176
L-homoserine
-
E237A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.0507
L-homoserine
-
K47M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.118
L-homoserine
-
K163M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.147
L-homoserine
-
E250A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.18
L-homoserine
-
E237Q, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.391
L-homoserine
-
E237D, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.4
L-homoserine
recombinant His-tagged mutant G52A/P55G enzyme, pH 8.0, 30°C
0.533
L-homoserine
-
S192A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
0.63
L-homoserine
recombinant His-tagged mutant P55G enzyme, pH 8.0, 30°C
0.692
L-homoserine
-
K47R, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
4.02
L-homoserine
-
E111G, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM succinyl-CoA, 25°C
4.56
L-homoserine
-
wild-type, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C
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evolution
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
evolution
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
evolution
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
evolution
-
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel
-
malfunction
-
enzyme enables the survival of fungi and bacteria in methionine-poor environments such as blood serum, thus its inhibition can be deleterious for the organism
malfunction
-
site-directed mutagenesis reveals that Bacillus cereus metA and Escherichia coli homoserine transsuccinylase share a common catalytic mechanism, glutamic acid 111 in the active site determines acetyl-CoA versus succinyl-CoA (glycine 111) specificity
metabolism
-
first step in the biosynthesis of methionine from aspartic acid
metabolism
-
methionine biosynthesis
metabolism
-
the enzyme reaction represents a critical control point for cell growth and viability
metabolism
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
metabolism
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
metabolism
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
physiological function
enzyme MsHAT catalyzes the transfer of acetyl-group from acetyl-CoA to homoserine
physiological function
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
physiological function
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
physiological function
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
enzyme MsHAT catalyzes the transfer of acetyl-group from acetyl-CoA to homoserine
-
additional information
the enzyme displays a high sequence homology to L-homoserine O-acetyltransferase, but it prefers L-serine over L-homoserine as the substrate, structure analysis and modeling, overview
additional information
-
the enzyme structure belongs to the alpha/beta-hydrolase superfamily, consisting of two distinct domains: a core alpha/beta-domain containing the catalytic site and a lid domain assembled into a helical bundle. The active site consists of a classical catalytic triad located at the end of a deep tunnel, structure comparisons, overview. The reaction catalyzed by the enzyme involves the acetylation of the gamma-hydroxyl of homoserine through an acetyl-CoA-dependent acetylation via a double-displacement mechanism facilitated by a classic Ser-His-Asp catalytic triad which is located at the bottom of a narrow tunnel
additional information
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(15-70), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
additional information
-
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(15-70), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
additional information
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium tuberculosis (MtMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(77-372), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
additional information
-
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium tuberculosis (MtMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(77-372), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
additional information
structure determination and comparison to structures of the Mycolicibacterium tuberculosis (MtMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(10-379), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
additional information
substrate binding mode and molecular mechanism of MsHAT, detailed overview. Enzyme structure comparisons. The active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HAT enzymes. The conserved Ser152, His345, and Asp315 residues form a catalytic triad, and they act as a covalent nucleophile, a general base, and an electron donor, respectively. Arg222, Asp346, Tyr229, and Tyr260 residues are mainly involved in the binding of homoserine or acetyl-CoA and other residues are not crucial for the stabilization of its substrates
additional information
-
substrate binding mode and molecular mechanism of MsHAT, detailed overview. Enzyme structure comparisons. The active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HAT enzymes. The conserved Ser152, His345, and Asp315 residues form a catalytic triad, and they act as a covalent nucleophile, a general base, and an electron donor, respectively. Arg222, Asp346, Tyr229, and Tyr260 residues are mainly involved in the binding of homoserine or acetyl-CoA and other residues are not crucial for the stabilization of its substrates
additional information
-
structure determination and comparison to structures of the Mycolicibacterium tuberculosis (MtMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(10-379), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium tuberculosis (MtMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(77-372), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium tuberculosis (MtMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(77-372), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
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additional information
-
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium tuberculosis (MtMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(77-372), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
structure determination and comparison to structures of the Mycolicibacterium tuberculosis (MtMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(10-379), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
structure determination and comparison to structures of the Mycolicibacterium tuberculosis (MtMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(10-379), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
structure determination and comparison to structures of the Mycolicibacterium tuberculosis (MtMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(10-379), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium tuberculosis (MtMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(77-372), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
structure determination and comparison to structures of the Mycolicibacterium tuberculosis (MtMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(10-379), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
structure determination and comparison to structures of the Mycolicibacterium tuberculosis (MtMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(10-379), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview
-
additional information
-
the enzyme displays a high sequence homology to L-homoserine O-acetyltransferase, but it prefers L-serine over L-homoserine as the substrate, structure analysis and modeling, overview
-
additional information
-
substrate binding mode and molecular mechanism of MsHAT, detailed overview. Enzyme structure comparisons. The active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HAT enzymes. The conserved Ser152, His345, and Asp315 residues form a catalytic triad, and they act as a covalent nucleophile, a general base, and an electron donor, respectively. Arg222, Asp346, Tyr229, and Tyr260 residues are mainly involved in the binding of homoserine or acetyl-CoA and other residues are not crucial for the stabilization of its substrates
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S143A
-
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
-
site-directed mutagenesis, the mutant shows an almost complete loss of activity
-
K267A
-
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
-
T56A
-
site-directed mutagenesis, the mutant shows a slight loss in activity
-
D209N
-
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
-
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
D403N
-
inactive mutant enzyme
H432A
-
inactive mutant enzyme
S163A
-
inactive mutant enzyme
S163C
-
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
-
site-directed mutagenesis, no activity with L-serine, but with L-homoserine, although the mutant is less active than the wild-type enzyme
-
P55G
-
site-directed mutagenesis, increased activity with L-serine and with L-homoserine compared to the wild-type enzyme
-
C142A
-
inactive enzyme
C142S
-
inactive enzyme
E111G
-
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
-
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
-
decrease in catalytic activity
E237A
-
compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
E237D
-
decrease in catalytic activity
E237D
-
compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
E237Q
-
decrease in catalytic activity
E237Q
-
compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
E250A
-
compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
E250A
-
13-14fold increase in homoserine Km value, homoserine binding is affected not acetyl-CoA binding
H235A
-
inactive enzyme
H235N
-
inactive enzyme
H235Q
-
inactive enzyme
K163M
-
compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
K163M
-
13-14fold increase in homoserine Km value, homoserine binding is affected not acetyl-CoA binding
K47M
-
compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
K47M
-
turnover number is reduced 14fold, Km value for acetyl-CoA is reduced 17fold, function in acetyl-CoA binding
K47R
-
compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
K47R
-
Km value for acetyl-CoA is affected, function in acetyl-CoA binding
R249M
-
compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
R249M
-
10fold reduction in kcat, 64fold higher Km for homoserine than wild-type, homoserine binding is affected not acetyl-CoA binding
S192A
-
compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
S192A
-
5fold increase in Km for homoserine, homoserine binding is affected not acetyl-CoA binding
additional information
-
Met auxotrophy is shown by a constructed MET2 mutant and its growth behavior in Met-deficient media
additional information
-
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
-
construction of truncated enzyme and isolated active site
additional information
construction of truncated enzyme and isolated active site
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
construction of truncated enzyme and isolated active site
additional information
-
construction of truncated enzyme and isolated active site
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
construction of truncated enzyme and isolated active site
-
additional information
-
methionine deficient strains do not perform the L-homoserine/O-acetyl-L-homoserine exchange reaction
additional information
-
methionine auxotroph strains show no activity
additional information
-
methionine auxotroph strains show no activity
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Yamagata, S.
Acetyl-CoA: L-homoserine O-acetyltransferase of the yeast Saccharomyces: substrate kinetics
Kyoyobu Kenkyu Hokoku
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27-28
1988
Paenibacillus polymyxa, [Brevibacterium] flavum, Saccharomyces cerevisiae
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Nagai, S.; Kerr, D.
Homoserine transacetylase (Neurospora)
Methods Enzymol.
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Neurospora sp.
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Miyajima, R.; Shiio, I.
Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. VII. Properities of homoserine O-transacetylase
J. Biochem.
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[Brevibacterium] flavum
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Wyman, A.; Paulus, H.
Purification and properties of homoserine transacetylase from Bacillus polymyxa
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3897-3903
1975
Paenibacillus polymyxa
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Langin, T.; Faugeron, G.; Goyon, C.; Nicolas, A.; Rossignol, J.L.
The MET2 gene of Saccharomyces cerevisiae: molecular cloning and nucleotide sequence
Gene
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1986
Saccharomyces cerevisiae
brenda
Yamagata, S.
Partial purification and some properties of homoserine O-acetyltransferase of a methionine auxotroph of Saccharomyces cerevisiae
J. Bacteriol.
169
3458-3463
1987
Saccharomyces cerevisiae
brenda
Goyon, C.; Faugeron, G.; Rossignol, J.L.
Molecular cloning and characterization of the met2 gene from Ascobolus immersus
Gene
63
297-308
1988
Ascobolus immersus
brenda
Nagai, S.; Flavin, M.
Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine
J. Biol. Chem.
242
3884-3895
1967
Neurospora sp.
brenda
Bourhy, P.; Martel, A.; Margarita, D.; Saint Girons, I.; Belfaiza, J.
Homoserine O-acetyltransferase, involved in the Leptospira meyeri methionine biosynthetic pathway, is not feedback inhibited
J. Bacteriol.
179
4396-4398
1997
Leptospira meyeri (P94891), Leptospira meyeri
brenda
Born, T.L.; Franklin, M.; Blanchard, J.S.
Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase
Biochemistry
39
8556-8564
2000
Haemophilus influenzae
brenda
Park, S.D.; Lee, J.Y.; Kim, Y.; Kim, J.H.; Lee, H.S.
Isolation and analysis of metA, a methionine biosynthetic gene encoding homoserine acetyltransferase in Corynebacterium glutamicum
Mol. Cell
8
286-294
1998
Corynebacterium glutamicum
brenda
Han, Y.K.; Lee, T.; Han, K.H.; Yun, S.H.; Lee, Y.W.
Functional analysis of the homoserine O-acetyltransferase gene and its identification as a selectable marker in Gibberella zeae
Curr. Genet.
46
205-212
2004
Fusarium graminearum
brenda
Nazi, I.; Wright, G.D.
Catalytic mechanism of fungal homoserine transacetylase
Biochemistry
44
13560-13566
2005
Schizosaccharomyces pombe
brenda
Mirza, I.A.; Nazi, I.; Korczynska, M.; Wright, G.D.; Berghuis, A.M.
Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases
Biochemistry
44
15768-15773
2005
Haemophilus influenzae (P45131), Haemophilus influenzae
brenda
Goudarzi, M.; Born, T.L.
Purification and characterization of Thermotoga maritima homoserine transsuccinylase indicates it is a transacetylase
Extremophiles
10
469-478
2006
Thermotoga maritima
brenda
Nazi, I.; Scott, A.; Sham, A.; Rossi, L.; Williamson, P.R.; Kronstad, J.W.; Wright, G.D.
Role of homoserine transacetylase as a new target for antifungal agents
Antimicrob. Agents Chemother.
51
1731-1736
2007
Cryptococcus neoformans
brenda
Wang, M.; Liu, L.; Wang, Y.; Wei, Z.; Zhang, P.; Li, Y.; Jiang, X.; Xu, H.; Gong, W.
Crystal structure of homoserine O-acetyltransferase from Leptospira interrogans
Biochem. Biophys. Res. Commun.
363
1050-1056
2007
Leptospira interrogans (Q8F4I0), Leptospira interrogans
brenda
Zubieta, C.; Arkus, K.A.; Cahoon, R.E.; Jez, J.M.
A single amino acid change is responsible for evolution of acyltransferase specificity in bacterial methionine biosynthesis
J. Biol. Chem.
283
7561-7567
2008
Bacillus cereus
brenda
De Pascale, G.; Nazi, I.; Harrison, P.H.; Wright, G.D.
beta-Lactone natural products and derivatives inactivate homoserine transacetylase, a target for antimicrobial agents
J. Antibiot.
64
483-487
2011
Haemophilus influenzae
brenda
Thangavelu, B.; Pavlovsky, A.G.; Viola, R.
Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure
Acta Crystallogr. Sect. F
70
1340-1345
2014
Staphylococcus aureus
brenda
Oda, K.; Matoba, Y.; Kumagai, T.; Noda, M.; Sugiyama, M.
Crystallographic study to determine the substrate specificity of an L-serine-acetylating enzyme found in the D-cycloserine biosynthetic pathway
J. Bacteriol.
195
1741-1749
2013
Streptomyces lavendulae (D2Z028), Streptomyces lavendulae ATCC 11924 (D2Z028)
brenda
Sagong, H.Y.; Hong, J.; Kim, K.J.
Crystal structure and biochemical characterization of O-acetylhomoserine acetyltransferase from Mycobacterium smegmatisATCC 19420
Biochem. Biophys. Res. Commun.
517
399-406
2019
Mycolicibacterium smegmatis (A0A8B4QGM8), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 19420 (A0A8B4QGM8)
brenda
Toelzer, C.; Pal, S.; Watzlawick, H.; Altenbuchner, J.; Niefind, K.
A novel esterase subfamily with alpha/beta-hydrolase fold suggested by structures of two bacterial enzymes homologous to L-homoserine O-acetyl transferases
FEBS Lett.
590
174-184
2016
no activity in Corynebacterium glutamicum, no activity in Pseudomonas veronii
brenda
Chaton, C.T.; Rodriguez, E.S.; Reed, R.W.; Li, J.; Kenner, C.W.; Korotkov, K.V.
Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site
Sci. Rep.
9
20267
2019
Mycobacteroides abscessus (B1MG17), Mycolicibacterium hassiacum (K5B926), Mycolicibacterium hassiacum, Mycobacterium tuberculosis (P9WJY9), Mycobacterium tuberculosis, Mycobacteroides abscessus JCM 13569 (B1MG17), Mycolicibacterium hassiacum DSM 44199 (K5B926), Mycolicibacterium hassiacum JCM 12690 (K5B926), Mycolicibacterium hassiacum CIP 105218 (K5B926), Mycobacteroides abscessus CIP 104536 (B1MG17), Mycobacteroides abscessus DSM 44196 (B1MG17), Mycobacteroides abscessus ATCC 19977 (B1MG17), Mycolicibacterium hassiacum 3849 (K5B926), Mycobacteroides abscessus NCTC 13031 (B1MG17), Mycobacteroides abscessus TMC 1543 (B1MG17)
brenda