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ATP + 4-hydroxynorvaline
ADP + 4-phospho-L-norvaline
-
0.3% of the activity with L-homoserine
-
-
?
ATP + D-homoserine
ADP + O-phospho-D-homoserine
-
32% of the turnover number with L-homoserine
-
-
?
ATP + L-2-amino-1,4-butanediol
ADP + ?
-
7.9% of the turnover number with L-homoserine
-
-
?
ATP + L-2-amino-5-hydroxyvalerate
ADP + L-2-amino-5-phosphovalerate
-
9.9% of the turnover number with L-homoserine
-
-
?
ATP + L-aspartate 4-semialdehyde
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
ATP + L-homoserine ethyl ester
ADP + O-phospho-L-homoserine ethyl ester
-
74% of the turnover number with L-homoserine
-
-
?
ATP + L-homoserine isopropyl ester
ADP + O-phospho-L-homoserine isopropyl ester
-
74% of the turnover number with L-homoserine
-
-
?
ATP + L-homoserine isubutyl ester
ADP + O-phospho-L-homoserine isobutyl ester
-
84% of the turnover number with L-homoserine
-
-
?
ATP + L-homoserine methyl ester
ADP + O-phospho-L-homoserine methyl ester
-
80% of the turnover number with L-homoserine
-
-
?
ATP + L-homoserine n-butyl ester
ADP + O-phospho-L-homoserine n-butyl ester
-
160% of the turnover number with L-homoserine
-
-
?
ATP + L-homoserine n-propyl ester
ADP + O-phospho-L-homoserine n-propyl ester
-
76% of the turnover number with L-homoserine
-
-
?
L-homoserine + ATP
O-phospho-L-homoserine + ADP
-
-
-
-
?
additional information
?
-
-
enzyme has inherent ATPase activity
-
-
?
ATP + L-aspartate 4-semialdehyde
?
-
8.2% of the turnover number with L-homoserine
-
-
?
ATP + L-aspartate 4-semialdehyde
?
-
10% of the activity with L-homoserine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
formation of O-phospho-L-homoserine, a branch point intermediate in the pathways for Met and Thr in plants
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
involved in the biosynthesis of threonine, isoleucine, and methionine, substrate availability rather than enzyme level rate limiting for the reaction
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme in the aspartate pathway of amino acid biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
key enzyme in the aspartate pathway of amino acid biosynthesis in E. coli
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
fourth enzyme in the aspartate pathway of amino acid biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme catalyzes a reaction common to synthesis of Thr, Ile and Met in plants
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme catalyzes an obligatory step of threonine biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme catalyzes a reaction common to synthesis of Thr, Ile and Met in plants
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme is a potential control point in the biosyntic pathway for Thr, Ile and Met
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme of L-Thr synthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme of L-Thr synthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme plays an important role in the regulation of the threonine biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme of threonine biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
involved in the biosynthesis of threonine and isoleucine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
involved in the biosynthesis of threonine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
involved in the biosynthesis of threonine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme is not involved in the regulation of methionine, threonine and isoleucine biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
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ATP + L-homoserine
ADP + O-phospho-L-homoserine
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
formation of O-phospho-L-homoserine, a branch point intermediate in the pathways for Met and Thr in plants
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
involved in the biosynthesis of threonine, isoleucine, and methionine, substrate availability rather than enzyme level rate limiting for the reaction
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme in the aspartate pathway of amino acid biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
key enzyme in the aspartate pathway of amino acid biosynthesis in E. coli
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
fourth enzyme in the aspartate pathway of amino acid biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme catalyzes a reaction common to synthesis of Thr, Ile and Met in plants
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme catalyzes an obligatory step of threonine biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme catalyzes a reaction common to synthesis of Thr, Ile and Met in plants
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme is a potential control point in the biosyntic pathway for Thr, Ile and Met
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme of L-Thr synthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme of L-Thr synthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme plays an important role in the regulation of the threonine biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
enzyme of threonine biosynthesis
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
involved in the biosynthesis of threonine and isoleucine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
involved in the biosynthesis of threonine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
involved in the biosynthesis of threonine
-
-
?
ATP + L-homoserine
ADP + O-phospho-L-homoserine
-
the enzyme is not involved in the regulation of methionine, threonine and isoleucine biosynthesis
-
?
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(1R,3r,5S)-8-[(1-cyclohexyl-1H-tetrazol-5-yl)methyl]-3-(pyridin-3-yl)-8-azabicyclo[3.2.1]octan-3-ol
-
(2S)-1-(9H-carbazol-9-yl)-3-(piperazin-1-yl)propan-2-ol
-
(2Z)-2-cyano-N-(2,5-dibromophenyl)-3-hydroxybut-2-enamide
-
-
(4R)-4-hydroxypentan-2-one
-
-
(naphthalen-1-yl)(1,3,5-triazatricyclo[3.3.1.13,7]decan-7-yl)methanone
-
(p-hydroxyphenyl)-glyoxal
-
-
1-(3,4-dihydroquinolin-1(2H)-yl)-2-[[1-(4-methylphenyl)-1H-tetrazol-5-yl]sulfanyl]ethan-1-one
-
1-(naphthalen-2-yl)prop-2-en-1-one
-
-
1-[(2R,6S)-2,6-dimethylpiperidin-1-yl]-2-[([1,2,4]triazolo[4,3-a]pyrimidin-3-yl)sulfanyl]ethan-1-one
-
1-[(2R,6S)-2,6-dimethylpiperidin-1-yl]-2-[4-(4-methylbenzoyl)piperidin-1-yl]ethan-1-one
-
2-(2-methylpropyl)-6,7,8,9-tetrahydro-4H,5H-cyclohepta[4,5]thieno[2,3-d][1,3]oxazin-4-one
-
-
2-(3,4-dihydroxyphenyl)-3,6,7-trihydroxy-2,3-dihydro-4H-chromen-4-one
-
-
2-amino-3-(phosphonoethyl)thiopropionate
-
-
2-Amino-5-phosphonovalerate
-
-
2-amino-5-phosphovalerate
-
-
2-[(5-amino-4-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]-N-(naphthalen-1-yl)acetamide
-
3-methyl-1-phenyl-6-(trifluoromethyl)-1H-pyrazolo[3,4-b]pyridin-4-ol
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,8a-dihydro-2H-chromen-3-yl)methyl]-2H-chromen-2-one
-
-
5'-adenylylimidodiphosphate
-
-
6-hydroxy-DL-Lys
-
5 mM, 92% inhibition
alpha-amino-beta-hydroxy valeric acid
-
-
L-2-amino-5-hydroxyvalerate
-
substrate inhibition
L-2-aminobutyric acid
-
40 mM, 50% inhibition
L-alpha-aminobutyric acid
-
-
L-Arg
-
10 mM, 13% inhibition
L-aspartate semialdehyde
-
mixed inhibition versus L-homoserine and ATP
L-homoserine alpha-methyl ester
-
substrate inhibition
L-homoserine ethyl ester
-
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
L-homoserine isopropyl ester
-
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
L-homoserine n-propyl ester
-
unlike the wild-type enzyme the mutant enzyme H202L is inhibited
L-Leu
-
10 mM, 20% inhibition
L-Lys
-
10 mM, 35% inhibition
L-Orn
-
10 mM, 64% inhibition
N,N'-(pyridine-2,5-diyl)dicyclohexanecarboxamide
-
N-[(3r)-adamantan-1-yl]-2-[3-(2-methylphenyl)-6-oxopyridazin-1(6H)-yl]acetamide
-
O-Phospho-DL-homoserine
-
10 mM, 91% inhibition
phosphohomoserine
-
inhibits phosphorylation of L-homoserine
pyridoxal 5'-phosphate
-
-
L-Cys
-
-
L-Cys
-
10 mM, 25% inhibition
L-homoserine
-
above 0.75 mM
L-homoserine
-
substrate inhibition
L-Ile
-
-
L-Ile
-
7.5 mM, 90% inhibition
L-Ile
-
no inhibition with the D-isomer
L-Met
-
-
L-Met
-
10 mM, 17% inhibition
L-Ser
-
-
L-Ser
-
10 mM, 10% inhibition
L-Thr
-
-
L-Thr
-
competitive to the substrate L-homoserine
L-Thr
-
substrate inhibition
L-Thr
-
10 mM, 18% inhibition
L-Thr
-
half-maximal inhibition at 10 mM
L-Thr
-
8.1 mM, 50% inhibition
L-threonine
competitive inhibition, interaction with ThrB residue A20 is important. Highly reduced inhibition of enzyme mutant A20G. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions
L-threonine
competitive inhibition
L-Val
-
-
L-Val
-
16 mM, 86% inhibition
S-adenosyl-L-methionine
-
10 mM, 92% inhibition
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
10 mM, 26% inhibition
additional information
-
no feedback inhibition by Thr, Met or Ile
-
additional information
virtual screening of a compound library and docking study, binding free energies, overview
-
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metabolism
downy mildew resistance is mediated by mutation of homoserine kinase: homoserine accumulation in the chloroplast triggers a novel form of downy mildew resistance
malfunction
-
deletion mutants show homoserine-mediated lethality
malfunction
-
deletion mutants show homoserine-mediated lethality
malfunction
-
homoserine kinase deletion mutants are attenuated in virulence and die rapidly upon threonine starvation and serum incubation
malfunction
-
homoserine kinase deletion mutants are extremely serum sensitive and hypersensitive to DNA-damaging agents
malfunction
mutations in the Arabidopsis homoserine kinase gene DMR1 confer enhanced resistance to Fusarium culmorum and Fusarium graminearum which cause Fusarium Ear Blight disease on small grain cereals
malfunction
-
deletion mutants show homoserine-mediated lethality
-
additional information
a conserved active-site alanine residue, A20, in CThrB (CglThrB) is important for differential interactions with L-threonine and L-homoserine
additional information
-
a conserved active-site alanine residue, A20, in CThrB (CglThrB) is important for differential interactions with L-threonine and L-homoserine
additional information
molecular modeling and simulation study of homoserine kinase (HSK) as an effective leishmanial drug target. Two MD simulations are performed on HSK enzyme without substrate (for reference), and on the enzyme in complex with the substrate, prosthetic group, and the magnesium ion using the NAMD program with CHARMM all-atom force field. The topology and parameters for the ligands used in this study are obtained from the MATCH web server. Virtual screening of a compound library and docking study. Homology modeling using several templates, overview. The active site of HSK mainly constitutes of two aspartates, two asparagine residues, and an arginine. All these residues are found to be optimally placed in the predicted model (Asn23, Asp29, Asp144, Asn145, and Arg241). Substrate recognition and structure-function analysis
additional information
-
a conserved active-site alanine residue, A20, in CThrB (CglThrB) is important for differential interactions with L-threonine and L-homoserine
-
additional information
-
a conserved active-site alanine residue, A20, in CThrB (CglThrB) is important for differential interactions with L-threonine and L-homoserine
-
additional information
-
a conserved active-site alanine residue, A20, in CThrB (CglThrB) is important for differential interactions with L-threonine and L-homoserine
-
additional information
-
a conserved active-site alanine residue, A20, in CThrB (CglThrB) is important for differential interactions with L-threonine and L-homoserine
-
additional information
-
a conserved active-site alanine residue, A20, in CThrB (CglThrB) is important for differential interactions with L-threonine and L-homoserine
-
additional information
-
a conserved active-site alanine residue, A20, in CThrB (CglThrB) is important for differential interactions with L-threonine and L-homoserine
-
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A20G
site-directed mutagenesis, the mutant retains wild-type enzymatic activity, with dramatically decreased feedback inhibition by L-threonine. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions
A20L
site-directed mutagenesis
A20S
site-directed mutagenesis
A20V
site-directed mutagenesis
A20G
-
site-directed mutagenesis, the mutant retains wild-type enzymatic activity, with dramatically decreased feedback inhibition by L-threonine. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions
-
A20L
-
site-directed mutagenesis
-
A20S
-
site-directed mutagenesis
-
A20V
-
site-directed mutagenesis
-
A20G
-
site-directed mutagenesis, the mutant retains wild-type enzymatic activity, with dramatically decreased feedback inhibition by L-threonine. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions
-
A20L
-
site-directed mutagenesis
-
A20S
-
site-directed mutagenesis
-
A20V
-
site-directed mutagenesis
-
A20G
-
site-directed mutagenesis, the mutant retains wild-type enzymatic activity, with dramatically decreased feedback inhibition by L-threonine. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions
-
A20L
-
site-directed mutagenesis
-
A20S
-
site-directed mutagenesis
-
A20V
-
site-directed mutagenesis
-
A20G
-
site-directed mutagenesis, the mutant retains wild-type enzymatic activity, with dramatically decreased feedback inhibition by L-threonine. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions
-
A20L
-
site-directed mutagenesis
-
A20S
-
site-directed mutagenesis
-
A20V
-
site-directed mutagenesis
-
A20G
-
site-directed mutagenesis, the mutant retains wild-type enzymatic activity, with dramatically decreased feedback inhibition by L-threonine. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions
-
A20L
-
site-directed mutagenesis
-
A20S
-
site-directed mutagenesis
-
A20V
-
site-directed mutagenesis
-
A20G
-
site-directed mutagenesis, the mutant retains wild-type enzymatic activity, with dramatically decreased feedback inhibition by L-threonine. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions
-
A20L
-
site-directed mutagenesis
-
A20S
-
site-directed mutagenesis
-
A20V
-
site-directed mutagenesis
-
H139L
-
mutant enzyme with diminished kinase activity and ATPase activity 150fold greater than that of the wild-type enzyme
H202L
-
Km-value for L-homoserine and ATP remain unchanged, the Ki-value for substrate inhibition by L-homoserine increases about 8fold, the turnover-number decreases by 50%,unlike the wild-type enzyme the L-homoserine ethyl, isopropyl, and n-propyl esters show substrate inhibition
H205Q
-
Km-value for ATP remains unchanged, ATPase activity is within a factor 2 of the wild-type enzyme, the kinase activity is less than 0.03% that of the wild-type enzyme
R234C
-
no observable homoserine kinase activity, the ATPase activity is nearly 20 times that of the wild-type enzyme at pH 8.0. 7fold increase in Km-value for ATP. Mutant enzyme is sensitive to heat treatment and begins to precipitate at 55°C
R234H
-
mutant enzyme has a diminished kinase activity, 0.4% of that of the wild-type enzyme, and an enhanced ATPase activity, Km-values for both substrates are unchanged
R234L
-
Km-value for L-homoserine increases nearly 300fold, the turnover-number decreases by 90fold compared to the wild-type enzyme. Less than a 2fold change in Km for ATP, the inherent ATPase activity increases by 3fold. The mutant enzyme has turnover-numbers for homoserine esters that are only 10% that of homoserine, but has higher affinity for the esters than for L-homoserine itself. L-Cys, a strong inhibitor of the wild-type enzyme, is 50fold less effective as inhibitor of the mutant enzyme. L-Thr no longer inhibits the mutant enzyme. Unlike the wild-type enzyme, addition of 10 mM L-homoserine to the mutant enzyme has no protective effect on the number of arginyl residues titrated with (p-hydroxyphenyl)glyoxal
additional information
six independent mutants of homoserine kinase (E46K, G118R, G180D, G202R, M241I, and A267V) are analyzed: 0-10% of wild-type activity
additional information
-
six independent mutants of homoserine kinase (E46K, G118R, G180D, G202R, M241I, and A267V) are analyzed: 0-10% of wild-type activity
additional information
engineering of Corynebacterium glutamicum to increase production of L-threonine, the attempt is to render the active site of Corynebacterium glutamicum ThrB (CglThrB) more selective toward L-homoserine than L-threonine
additional information
-
engineering of Corynebacterium glutamicum to increase production of L-threonine, the attempt is to render the active site of Corynebacterium glutamicum ThrB (CglThrB) more selective toward L-homoserine than L-threonine
additional information
-
engineering of Corynebacterium glutamicum to increase production of L-threonine, the attempt is to render the active site of Corynebacterium glutamicum ThrB (CglThrB) more selective toward L-homoserine than L-threonine
-
additional information
-
engineering of Corynebacterium glutamicum to increase production of L-threonine, the attempt is to render the active site of Corynebacterium glutamicum ThrB (CglThrB) more selective toward L-homoserine than L-threonine
-
additional information
-
engineering of Corynebacterium glutamicum to increase production of L-threonine, the attempt is to render the active site of Corynebacterium glutamicum ThrB (CglThrB) more selective toward L-homoserine than L-threonine
-
additional information
-
engineering of Corynebacterium glutamicum to increase production of L-threonine, the attempt is to render the active site of Corynebacterium glutamicum ThrB (CglThrB) more selective toward L-homoserine than L-threonine
-
additional information
-
engineering of Corynebacterium glutamicum to increase production of L-threonine, the attempt is to render the active site of Corynebacterium glutamicum ThrB (CglThrB) more selective toward L-homoserine than L-threonine
-
additional information
-
engineering of Corynebacterium glutamicum to increase production of L-threonine, the attempt is to render the active site of Corynebacterium glutamicum ThrB (CglThrB) more selective toward L-homoserine than L-threonine
-
additional information
-
gene is essential for growth in rich media, when ammonium is the nitrogen source, or when threonine is supplied as an amino acid instead of a dipeptide. the severity of the growth defect associated with THR1 repression increases with increasing incubation temperature
additional information
-
expression in Solanum tuberosum plant with targeting to chloroplast and cytosol. Both approaches result in up to 11fold increase in total enzyme activity. Transgenic plants exhibit reduced homoserine levels while methionine and threonine do not accumulate significantly. Plants with elevated levels of cytosolic enzyme exhibit a reduction in transcript levels of the endogenous homoserine kinase, as well as of threonine synthase, cystathionine beta-lyase, and methionine synthase. In all plants, cystathionine gamma-synthase expression remains unchanged, while S-adenosylmethionine synthetase expression increases. Excess of plastidial localized homoserine kinase does not influence the de novo synthesis of methionine and threonine
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Corynebacterium glutamicum (P07128), Corynebacterium glutamicum, Corynebacterium glutamicum LMG 3730 (P07128), Corynebacterium glutamicum BCRC 11384 (P07128), Corynebacterium glutamicum ATCC 13032 (P07128), Corynebacterium glutamicum JCM 1318 (P07128), Corynebacterium glutamicum NCIMB 10025 (P07128), Corynebacterium glutamicum DSM 20300 (P07128)
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Leishmania major (Q4Q6Y2)
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