Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
glutaryl-CoA + L-homoserine
CoA + O-glutaryl-L-homoserine
-
-
-
-
r
succinyl-CoA + D-homoserine
CoA + O-succinyl-D-homoserine
-
-
-
-
r
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
additional information
?
-
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
r
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
involved in cystathionine and methionine biosynthesis
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
involved in cystathionine and methionine biosynthesis
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
involved in cystathionine and methionine biosynthesis
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
a step in biosynthesis and regulation of methionine, overview
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
step in the biosynthetic pathways of methionine and S-adenosylmethionine, overview
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
a step in biosynthesis and regulation of methionine, overview
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
additional information
?
-
-
3-amino-1-propanol, L-serine, and L-threonine are poor substrates
-
-
?
additional information
?
-
-
no activity with acetyl-CoA, propionyl-CoA, butyryl-CoA, crotonyl-CoA, malonyl-CoA, and gamma-hydroxybutyric acid, and gamma-aminobutyric acid
-
-
?
additional information
?
-
-
the enzyme is important in regulation of Met biosynthesis and metabolism, metA expression is regulated by the methionine repressor metJ, MetJ and MetA enzyme mutations lead to pathway deregulation and excess methionine production and excretion from the cell, overview
-
-
?
additional information
?
-
-
the enzyme is important in regulation of Met biosynthesis and metabolism, metA expression is regulated by the methionine repressor metJ, MetJ and MetA enzyme mutations lead to pathway deregulation and excess methionine production and excretion from the cell, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
additional information
?
-
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
involved in cystathionine and methionine biosynthesis
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
involved in cystathionine and methionine biosynthesis
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
involved in cystathionine and methionine biosynthesis
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
a step in biosynthesis and regulation of methionine, overview
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
step in the biosynthetic pathways of methionine and S-adenosylmethionine, overview
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
a step in biosynthesis and regulation of methionine, overview
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
-
-
-
?
additional information
?
-
-
the enzyme is important in regulation of Met biosynthesis and metabolism, metA expression is regulated by the methionine repressor metJ, MetJ and MetA enzyme mutations lead to pathway deregulation and excess methionine production and excretion from the cell, overview
-
-
?
additional information
?
-
-
the enzyme is important in regulation of Met biosynthesis and metabolism, metA expression is regulated by the methionine repressor metJ, MetJ and MetA enzyme mutations lead to pathway deregulation and excess methionine production and excretion from the cell, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.64
coenzyme A
-
recombinant protein
10
D-homoserine
-
recombinant protein
0.18
glutaryl-CoA
-
recombinant protein
0.0032 - 95.5
L-homoserine
3.5
O-succinylhomoserine
-
recombinant protein
additional information
additional information
-
0.0032
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K47A
0.027
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K46R/K47R
0.044
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K46A
0.044
L-homoserine
-
pH 7.5, 25°C, recombinant mutant K45L
0.049
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K47R
0.31
L-homoserine
-
pH 7.5, 25°C, recombinant mutant R193K
0.36
L-homoserine
-
pH 7.5, 25°C, recombinant mutant E237D
0.38
L-homoserine
-
pH 7.5, 25°C, recombinant wild-type enzyme
0.58
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K46R
0.72
L-homoserine
-
pH 7.2, 25°C, recombinant wild-type enzyme
0.83
L-homoserine
recombinant His-tagged mutant I124L, pH and temperature not specified in the publication
1.07
L-homoserine
-
pH 7.2, 25°C, recombinant mutant C90S
1.1
L-homoserine
-
pH 7.5, 25°C, recombinant mutant E237A
1.1
L-homoserine
-
pH 7.5, 25°C, recombinant mutant R193A
1.15
L-homoserine
-
pH 7.5, 25°C, recombinant mutant R249A
1.25
L-homoserine
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
1.42
L-homoserine
recombinant His-tagged mutant I229Y, pH and temperature not specified in the publication
1.51
L-homoserine
-
pH 7.5, 25°C, recombinant mutant R249K
1.6
L-homoserine
-
recombinant protein
2
L-homoserine
-
pH 7.5, 25°C, recombinant mutant Y238F
2.26
L-homoserine
-
pH 7.5, 25°C, recombinant mutant K46L
9.1
L-homoserine
-
pH 7.5, 25°C, recombinant mutant E246D
59.1
L-homoserine
-
pH 7.5, 25°C, recombinant mutant E246A
93.8
L-homoserine
-
pH 7.5, 25°C, recombinant mutant R193A/E246A
95.5
L-homoserine
-
pH 7.5, 25°C, recombinant mutant Y238F/E246A
0.043
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant E246D
0.05
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant Y238F/E246A
0.094
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K47R
0.094
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant E246A
0.13
succinyl-CoA
-
pH 7.2, 25°C, recombinant wild-type enzyme
0.13
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K46R
0.13
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K46R/K47R
0.14
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant C90S
0.14
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K46A
0.15
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant E237A
0.16
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K47A
0.17
succinyl-CoA
-
recombinant protein
0.2
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R193A/E246A
0.23
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R249A
0.24
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant E237D
0.28
succinyl-CoA
-
pH 7.5, 25°C, recombinant wild-type enzyme
0.31
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R249K
0.35
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant Y238F
0.36
succinyl-CoA
recombinant His-tagged mutant I229Y, pH and temperature not specified in the publication
0.37
succinyl-CoA
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
0.38
succinyl-CoA
recombinant His-tagged mutant I124L, pH and temperature not specified in the publication
0.4
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R193K
0.43
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R193A
1.78
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant K46L
2.9
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant K45L
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
-
steady-state kinetics and thermodynamics of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.23
coenzyme A
-
recombinant protein
12
D-homoserine
-
recombinant protein
1.6
glutaryl-CoA
-
recombinant protein
5.23
O-succinyl-L-homoserine
-
recombinant protein
0.034
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K47A
1.8
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K47R
2
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K46R/K47R
4.1
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K46A
24
L-homoserine
-
recombinant protein
36.72
L-homoserine
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
37
L-homoserine
-
pH 7.2, 25°C, recombinant mutant K46R
38.59
L-homoserine
recombinant His-tagged mutant I124L, pH and temperature not specified in the publication
39.28
L-homoserine
recombinant His-tagged mutant I229Y, pH and temperature not specified in the publication
130
L-homoserine
-
pH 7.2, 25°C, recombinant wild-type enzyme
130
L-homoserine
-
pH 7.2, 25°C, recombinant mutant C90S
0.34
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K47A
0.8
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant E237A
1.2
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R193A/E246A
1.26
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant K46L
1.8
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K47R
2
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K46R/K47R
2 - 3.7
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R249K
3.3
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R193A
3.4
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R193K
4.1
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K46A
6.7
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant E237D
6.9
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant E246A
8.9
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant Y238F/E246A
10
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant R249A
13
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant Y238F
15
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant E246D
24
succinyl-CoA
-
recombinant protein
25.7
succinyl-CoA
-
pH 7.5, 25°C, recombinant wild-type enzyme
36.72
succinyl-CoA
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
37
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant K46R
38.59
succinyl-CoA
recombinant His-tagged mutant I124L, pH and temperature not specified in the publication
39.28
succinyl-CoA
recombinant His-tagged mutant I229Y, pH and temperature not specified in the publication
40.1
succinyl-CoA
-
pH 7.5, 25°C, recombinant mutant K45L
130
succinyl-CoA
-
pH 7.2, 25°C, recombinant wild-type enzyme
130
succinyl-CoA
-
pH 7.2, 25°C, recombinant mutant C90S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A195T
site-directed mutagenesis
A200E
site-directed mutagenesis
A28V
the mutation leads to 2.94fold improved L-methionine productivity in Escherichia coli DELTAIJA strain
C142A
-
site-directed mutagenesis, the mutant is inactive
C90A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
C90S
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
D218G
site-directed mutagenesis
E213V
-
15-20% faster growth at 36-41°C, lower growth rate at 44°C (64% of control), no growth at 45°C
E237A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E237D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E246A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E246D
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency with L-homoserine, but increased with succinyl-CoA compared to the wild-type enzyme
F247Y
site-directed mutagenesis, the mutant shows accelerated growth at 44°C in M9 glucose medium in contrast to the wild-type
H235A
-
site-directed mutagenesis, the mutant is inactive
I124L
site-directed mutagenesis, the mutant shows accelerated growth at 44°C in M9 glucose medium in contrast to the wild-type
I124L-I229Y
site-directed mutagenesis, the mutant shows highly accelerated growth at 44°C in M9 glucose medium in contrast to the wild-type
I124L-I229Y-N267D
site-directed mutagenesis, the mutant shows highly accelerated growth at 44°C in M9 glucose medium in contrast to the wild-type
I229T
-
normal growth at 37°C, better growth at 44°C compared to control, 48% faster growth at 44°C, 18% faster growth at 43°C, no growth at 45°C, 1.4times greater cell density with 30 mM acetic acid at 30°C than control, heating at 45°C for 40 min reduces soluble enzyme to 29% compared to unheated culture, increases insoluble enzyme content 13-19times, 3 h incubation in 30 mM acetic acid at 30°C shows 1.5-3times higher levels of soluble enzyme than the wild-type strain and 2.6times higher insoluble enzyme levels
I299Y
site-directed mutagenesis, the mutant shows accelerated growth at 44°C in M9 glucose medium in contrast to the wild-type
K156L
-
site-directed mutagenesis, the mutant is inactive
K45L
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K46A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K46L
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K46R
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K46R/K47R
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K47A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K47R
-
site-directed mutagenesis, the mutant shows 90% reduced activity compared to the wild-type enzyme
L110V
site-directed mutagenesis
L63F
the mutation leads to 2.91fold improved L-methionine productivity in Escherichia coli DELTAIJA strain
L63F/A28V
the mutations lead to 4.3fold improved L-methionine productivity in Escherichia coli DELTAIJA strain
N271K
-
15-20% faster growth at 36-41°C, lower growth rate at 44°C (22% of control), no growth at 45°C
Q64E
the mutation leads to improved L-methionine productivity in Escherichia coli DELTAIJA strain
Q96K
site-directed mutagenesis, the mutant shows accelerated growth at 44°C in M9 glucose medium in contrast to the wild-type
R160L
site-directed mutagenesis
R193A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R193A/E246A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency with L-homoserine and reduced activity with succinyl-CoA compared to the wild-type enzyme
R193K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R249A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R249K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S61T/E213V/I229T/N267D/N271K
-
introduction of random mutagenesis by error-prone PCR, fast growing strain at 44°C, 5-12% faster growing than control strain at a temperature range from 30-42°C, at 43°C 30% faster growth, at 44°C 64% faster growth, no growth at 45°C, 1.4fold slower growth in methionine deficient medium at 43 and 44°C compared to 1.6 and 2fold slowing in the wild-type, 1.4times greater cell density with 30 mM acetic acid at 30°C than control, heating at 45°C for 40 min reduces soluble enzyme to 58% compared to unheated culture, increases insoluble enzyme content 13-19times, 3 h incubation in 30 mM acetic acid at 30°C shows 1.5-3times higher levels of soluble enzyme than the wild-type strain and 9times higher insoluble enzyme levels
Y238F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y238F/E246A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency with L-homoserine, but increased with succinyl-CoA compared to the wild-type enzyme
I296S
-
point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A4
-
P298L
-
point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A5
-
R27C
-
point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A9
-
C142S
-
site-directed mutagenesis, the mutant is almost inactive
C142S
-
site-directed mutagenesis, the mutant is inactive
H235N
-
site-directed mutagenesis, the mutant is almost inactive
H235N
-
site-directed mutagenesis, the mutant is inactive
I296S
-
point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A4
I296S
the mutation leads to improved L-methionine productivity in Escherichia coli DELTAIJA strain
K45A/K46A
-
no residual enzyme activity, strain is auxotroph for L-methionine
K45A/K46A
-
site-directed mutagenesis, the mutant is inactive
K45A/K46A
-
site-directed mutagenesis, the mutant is nearly inactive
N267D
-
normal growth at 37°C, better growth at 44°C compared to control, 31% faster growth at 44°C, 10% faster growth at 43°C, no growth at 45°C, with 30 mM acetic acid at 30°C slower growth than other thermostable strains and only 16% higher cell density than control, heating at 45°C for 40 min reduces soluble enzyme to 67% compared to unheated culture, increases insoluble enzyme content 13-19times, 3 h incubation in 30 mM acetic acid at 30°C shows 1.5-3times higher levels of soluble enzyme than the wild-type strain and 8times higher insoluble enzyme levels
N267D
the mutation leads to improved L-methionine productivity in Escherichia coli DELTAIJA strain
P298L
-
point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A5
P298L
the mutation leads to 2.89fold improved L-methionine productivity in Escherichia coli DELTAIJA strain
R27C
-
point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A9
R27C
the mutation leads to improved L-methionine productivity in Escherichia coli DELTAIJA strain
S61T
-
similar growth rate as mutants E213V and N271K at 36-41°C (15-20% faster), similar growth as wild-type at elevated temperatures, no growth at 45°C
S61T
the mutation leads to improved L-methionine productivity in Escherichia coli DELTAIJA strain
additional information
-
construction of IS-insertion mutant metA7, with 298Pro-Tyr-Asp-Leu-Arg-His-Met-Asn-Pro-Thr-Leu-Asp-stop to 298Arg-Leu-Ala-Pro-stop, obtained from norleucine-resistant strain, and IS insertion mutant metA8, with 298Pro-Tyr-Asp-Leu-Arg-His-Met-Asn-Pro-Thr-Leu-Asp-stop to 298Arg-Leu-Ala-Pro-stop, also obtained from norleucine-resistant strain, overview, introduction of deletion mutations of metJ and thrBC into the W3110 strain has a significant effect on the amount of Met excreted into the medium, overview
additional information
-
wild-type Escherichia coli enzyme, normal growth at 37°C, less growth than the mutants at 44°C no growth at 45°C, heating at 45°C for 40 min reduces soluble enzyme to 35% compared to unheated culture, increases insoluble enzyme content 44times, 3 h incubation in 30 mM acetic acid at 30°C shows 1.5-3times lower levels of soluble enzyme than the mutants and 15times higher insoluble enzyme levels
additional information
stabilized MetA mutant enzymes at least partially recover the growth defects of mutant Escherichia coli strains with deletions of either ATP-dependent proteases or the DnaK chaperone, increased accumulation of insoluble wild-type MetA in heat-stressed DELTAdnaK cells compared with the mutated I124L and I229Y enzymes, which have relative amounts of 57% and 33% of the wild-type enzyme, respectively
additional information
-
stabilized MetA mutant enzymes at least partially recover the growth defects of mutant Escherichia coli strains with deletions of either ATP-dependent proteases or the DnaK chaperone, increased accumulation of insoluble wild-type MetA in heat-stressed DELTAdnaK cells compared with the mutated I124L and I229Y enzymes, which have relative amounts of 57% and 33% of the wild-type enzyme, respectively
additional information
the enzyme is prone to aggregation under many stress conditions, resulting in a methionine limitation in Escherichia coli growth. Overexpression of MetA induces the greatest number of persisters at 42°C, which is correlated to an increased level of aggregated MetA. Substitution of the native metA gene on the Escherichia coli K-12 WE chromosome by a mutant gene encoding the stabilized MetA leads to reduction in persisters at the elevated temperature and in the presence of acetate, as well as lower aggregation of the mutated MetA. Decreased persister formation at 42°C is confirmed also in wild-type Escherichia coli K-12 W3110 and a fast-growing WErph+ mutant harboring the stabilized MetA. The frequency of persister formation is correlated to the aggregation of the MetA, more than 150fold increase in the frequency of persisters at 42°C result from an increased level of aggregated proteins. Stabilized MetA reduces persister formation in the presence of acetate
additional information
-
the enzyme is prone to aggregation under many stress conditions, resulting in a methionine limitation in Escherichia coli growth. Overexpression of MetA induces the greatest number of persisters at 42°C, which is correlated to an increased level of aggregated MetA. Substitution of the native metA gene on the Escherichia coli K-12 WE chromosome by a mutant gene encoding the stabilized MetA leads to reduction in persisters at the elevated temperature and in the presence of acetate, as well as lower aggregation of the mutated MetA. Decreased persister formation at 42°C is confirmed also in wild-type Escherichia coli K-12 W3110 and a fast-growing WErph+ mutant harboring the stabilized MetA. The frequency of persister formation is correlated to the aggregation of the MetA, more than 150fold increase in the frequency of persisters at 42°C result from an increased level of aggregated proteins. Stabilized MetA reduces persister formation in the presence of acetate
additional information
-
construction of IS-insertion mutant metA7, with 298Pro-Tyr-Asp-Leu-Arg-His-Met-Asn-Pro-Thr-Leu-Asp-stop to 298Arg-Leu-Ala-Pro-stop, obtained from norleucine-resistant strain, and IS insertion mutant metA8, with 298Pro-Tyr-Asp-Leu-Arg-His-Met-Asn-Pro-Thr-Leu-Asp-stop to 298Arg-Leu-Ala-Pro-stop, also obtained from norleucine-resistant strain, overview, introduction of deletion mutations of metJ and thrBC into the W3110 strain has a significant effect on the amount of Met excreted into the medium, overview
-
additional information
-
the recombinant Geobacillus kaustophilus enzyme stimulates Escherichia coli growth at 44°C (20% faster than control) but inhibits growth by 20% at 37°C compared to the wild-type, between 30-42°C growth is inhibited by about 10%, at 43°C growth is equal to the Escherichia coli wild-type enzyme
additional information
-
the recombinant Geobacillus kaustophilus enzyme stimulates Escherichia coli growth at 44°C (20% faster than control) but inhibits growth by 20% at 37°C compared to the wild-type, between 30-42°C growth is inhibited by about 10%, at 43°C growth is equal to the Escherichia coli wild-type enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Rowbury, R.J.; Woods, D.D.
O-Succinyl-homoserine as an intermediate in the synthesis of cystathionine by Escherichia coli
J. Gen. Microbiol.
36
341-358
1964
Escherichia coli
brenda
Rhl, F.; Rabenhorst, J.; Zhner, H.
Biological properties and mode of action of clavams
Arch. Microbiol.
147
315-320
1987
Escherichia coli
brenda
Mares, R.; Urbanowski, M.L.; Stauffer, G.V.
Regulation of the Salmonella typhimurium metA gene by the metR protein and homocysteine
J. Bacteriol.
174
390-397
1992
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Born, T.L.; Blanchard, J.S.
Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase
Biochemistry
38
14416-14423
1999
Escherichia coli
brenda
Rosen, R.; Becher, D.; Buttner, K.; Biran, D.; Hecker, M.; Ron, E.Z.
Probing the active site of homoserine trans-succinylase
FEBS Lett.
577
386-392
2004
Escherichia coli
brenda
Usuda, Y.; Kurahashi, O.
Effects of deregulation of methionine biosynthesis on methionine excretion in Escherichia coli
Appl. Environ. Microbiol.
71
3228-3234
2005
Escherichia coli, Escherichia coli W3110 / ATCC 27325
brenda
Coe, D.M.; Viola, R.E.
Assessing the roles of essential functional groups in the mechanism of homoserine succinyltransferase
Arch. Biochem. Biophys.
461
211-218
2007
Escherichia coli
brenda
Ziegler, K.; Noble, S.M.; Mutumanje, E.; Bishop, B.; Huddler, D.P.; Born, T.L.
Identification of catalytic cysteine, histidine, and lysine residues in Escherichia coli homoserine transsuccinylase
Biochemistry
46
2674-2683
2007
Escherichia coli
brenda
Zubieta, C.; Krishna, S.S.; McMullan, D.; Miller, M.D.; Abdubek, P.; Agarwalla, S.; Ambing, E.; Astakhova, T.; Axelrod, H.L.; Carlton, D.; Chiu, H.; Clayton, T.; Deller, M.; DiDonato, M.; Duan, L.; Elsliger, M.; Grzechnik, S.K.; Hale, J.; Hampton, E.; Han, G.W.; Haugen, J.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Koesema, E.; Kumar, A.; Marciano, D.; Morse, A.T.; Nigoghossian, E.; Oommachen, S.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Weekes, D.; White, A.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4.ANG. resolution
Proteins Struct. Funct. Bioinform.
68
999-1005
2007
Bacillus cereus (Q72X44), Bacillus cereus
brenda
Mordukhova, E.A.; Lee, H.S.; Pan, J.G.
Improved thermostability and acetic acid tolerance of Escherichia coli via directed evolution of homoserine o-succinyltransferase
Appl. Environ. Microbiol.
74
7660-7668
2008
Escherichia coli, Geobacillus kaustophilus, Geobacillus kaustophilus KCTC 3397
brenda
Mordukhova, E.A.; Kim, D.; Pan, J.G.
Stabilized homoserine O-succinyltransferases (MetA) or L-methionine partially recovers the growth defect in Escherichia coli lacking ATP-dependent proteases or the DnaK chaperone
BMC Microbiol.
13
179
2013
Escherichia coli (P07623), Escherichia coli
brenda
Mordukhova, E.A.; Pan, J.G.
Stabilization of homoserine-O-succinyltransferase (MetA) decreases the frequency of persisters in Escherichia coli under stressful conditions
PLoS ONE
9
e110504
2014
Escherichia coli (P07623), Escherichia coli
brenda
Huang, J.F.; Zhang, B.; Shen, Z.Y.; Liu, Z.Q.; Zheng, Y.G.
Metabolic engineering of E. coli for the production of O-succinyl-L-homoserine with high yield
3 Biotech
8
310
2018
Escherichia coli (P07623)
brenda
Tang, X.L.; Chen, L.J.; Du, X.Y.; Zhang, B.; Liu, Z.Q.; Zheng, Y.G.
Regulation of homoserine O-succinyltransferase for efficient production of L-methionine in engineered Escherichia coli
J. Biotechnol.
309
53-58
2020
Escherichia coli (P07623), Escherichia coli
brenda