2.3.1.46: homoserine O-succinyltransferase
This is an abbreviated version!
For detailed information about homoserine O-succinyltransferase, go to the full flat file.
Word Map on EC 2.3.1.46
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2.3.1.46
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chaperone
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acyltransferases
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refolding
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noncanonical
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cereus
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threonine
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biotechnology
- 2.3.1.46
- chaperone
- acyltransferases
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refolding
-
noncanonical
- cereus
- threonine
- biotechnology
Reaction
Synonyms
homoserine O-succinyltransferase, homoserine O-transsuccinylase, homoserine succinyltransferase, homoserine transsuccinylase, homoserine-O-succinyltransferase, HST, HTS, MetA, MetA protein, succinyltransferase, homoserine
ECTree
2.3.1.46 homoserine O-succinyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.3.1.46 - homoserine O-succinyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A28V
the mutation leads to 2.94fold improved L-methionine productivity in Escherichia coli DELTAIJA strain
C142S
C90A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
C90S
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
E213V
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15-20% faster growth at 36-41°C, lower growth rate at 44°C (64% of control), no growth at 45°C
E237A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E237D
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E246A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E246D
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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
H235N
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
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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
I296S
I299Y
site-directed mutagenesis, the mutant shows accelerated growth at 44°C in M9 glucose medium in contrast to the wild-type
K45A/K46A
K45L
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K46A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K46L
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K46R
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K46R/K47R
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K47A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K47R
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site-directed mutagenesis, the mutant shows 90% reduced activity compared to the wild-type enzyme
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
N267D
N271K
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15-20% faster growth at 36-41°C, lower growth rate at 44°C (22% of control), no growth at 45°C
P298L
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
R193A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R193A/E246A
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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
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R249A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R249K
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R27C
S61T
S61T/E213V/I229T/N267D/N271K
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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
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y238F/E246A
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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
Escherichia coli W3110 / ATCC 27325
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point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A4
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P298L
Escherichia coli W3110 / ATCC 27325
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point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A5
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R27C
Escherichia coli W3110 / ATCC 27325
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point mutation in gene metA leading to a deregulated methionine biosynthesis in the mutant strain A9
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additional information
I296S
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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
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no residual enzyme activity, strain is auxotroph for L-methionine
N267D
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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
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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
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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
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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
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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
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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
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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
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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
Escherichia coli W3110 / ATCC 27325
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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
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additional information
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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
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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
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