2.7.1.39: homoserine kinase
This is an abbreviated version!
For detailed information about homoserine kinase, go to the full flat file.
Word Map on EC 2.7.1.39
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2.7.1.39
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keratitis
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herpes
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simplex
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corneal
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herpetic
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horseshoe
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immunopathological
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keratoplasty
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opacity
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virus-1
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immunoinflammatory
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isthmus
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trigeminal
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hsv-specific
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acyclovir
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anti-hsv
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phosphomevalonate
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agriculture
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slit-lamp
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aspartokinase
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drug development
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nephrolithotomy
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transperitoneal
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stone-free
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mckrae
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medicine
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lithotripsy
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hsv-infected
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hsv-1-induced
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lactofermentum
- 2.7.1.39
- keratitis
-
herpes
- simplex
- corneal
-
herpetic
-
horseshoe
-
immunopathological
-
keratoplasty
- opacity
-
virus-1
-
immunoinflammatory
-
isthmus
-
trigeminal
-
hsv-specific
- acyclovir
-
anti-hsv
- phosphomevalonate
- agriculture
-
slit-lamp
- aspartokinase
- drug development
-
nephrolithotomy
-
transperitoneal
-
stone-free
-
mckrae
- medicine
-
lithotripsy
-
hsv-infected
-
hsv-1-induced
- lactofermentum
Reaction
Synonyms
CglThrB, CThrB, DMR1, homoserine kinase, homoserine kinase (phosphorylating), HSK, kinase (phosphorylating), homoserine, kinase, homoserine (phosphorylating), Thr1, Thr1p, ThrB
ECTree
2.7.1.39 homoserine kinaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.7.1.39 - homoserine kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
A20G
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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
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A20G
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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
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A20G
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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
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A20G
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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
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A20G
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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
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A20G
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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
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H139L
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mutant enzyme with diminished kinase activity and ATPase activity 150fold greater than that of the wild-type enzyme
H202L
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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
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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
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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
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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
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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
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
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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
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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
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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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
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additional information
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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
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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
