Information on EC 2.7.1.39 - homoserine kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.7.1.39
-
RECOMMENDED NAME
GeneOntology No.
homoserine kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + L-homoserine = ADP + O-phospho-L-homoserine
show the reaction diagram
ordered random mechanism with ATP preferentially binding before L-homoserine
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ATP + L-homoserine = ADP + O-phospho-L-homoserine
show the reaction diagram
rapid equilibrium random bi bi mechanism
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ATP + L-homoserine = ADP + O-phospho-L-homoserine
show the reaction diagram
the catalytic mechanism of the enzyme does not involve a catalytic base for activating the phosphoryl acceptor hydroxyl but instead is mediated via a transition state stabilization mechanism
Q58504
ATP + L-homoserine = ADP + O-phospho-L-homoserine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
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Metabolic pathways
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methionine biosynthesis II
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Microbial metabolism in diverse environments
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threonine biosynthesis from homoserine
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SYSTEMATIC NAME
IUBMB Comments
ATP:L-homoserine O-phosphotransferase
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homoserine kinase
Q8L7R2
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homoserine kinase
-
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homoserine kinase (phosphorylating)
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-
-
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HSK
-
-
-
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kinase (phosphorylating), homoserine
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-
-
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kinase, homoserine (phosphorylating)
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-
-
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Thr1
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gene name
Thr1
-
gene name
Thr1
-
gene name
-
CAS REGISTRY NUMBER
COMMENTARY
9026-58-8
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TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
14.2
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ATP
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in 50 mM HEPES, pH 7.5, 40 mM KCl, 10 mM MgCl2, at 37C
40.8
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ATP
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pH 7.5, 30C
3.3
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D-homoserine
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wild-type enzyme
2
-
L-2-amino-1,4-butanediol
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wild-type enzyme
2.5
-
L-2-amino-5-hydroxyvalerate
-
wild-type enzyme
2.1
-
L-aspartate beta-semialdehyde
-
wild-type enzyme
0.2
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L-homoserine
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mutant R234L
0.75
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L-homoserine
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method: isothermal titration calometry
9.1
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L-homoserine
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mutant H202L
11.2
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L-homoserine
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in 50 mM HEPES, pH 7.5, 40 mM KCl, 10 mM MgCl2, at 37C
18.3
-
L-homoserine
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wild-type enzyme
40.2
-
L-homoserine
-
pH 7.5, 30C
0.007
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L-homoserine butyl ester
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mutant R234L
2.5
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L-homoserine butyl ester
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mutant H202L
0.021
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L-homoserine ethyl ester
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mutant R234L
4.1
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L-homoserine ethyl ester
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mutant H202L
13.6
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L-homoserine ethyl ester
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wild-type enzyme
16.4
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L-homoserine isobutyl ester
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wild-type enzyme
13.6
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L-homoserine isopropyl ester
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wild-type enzyme
0.018
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L-homoserine methyl ester
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mutant R234L
5.4
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L-homoserine methyl ester
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mutant H202L
14.7
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L-homoserine methyl ester
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wild-type enzyme
29.1
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L-homoserine n-butyl ester
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wild-type enzyme
14
-
L-homoserine n-propyl ester
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wild-type enzyme
0.0111
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L-homoserine propyl ester
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mutant R234L
2.7
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L-homoserine propyl ester
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mutant H202L
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
210
-
ATP
-
in 50 mM HEPES, pH 7.5, 40 mM KCl, 10 mM MgCl2, at 37C
22040
24.1
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L-homoserine
-
in 50 mM HEPES, pH 7.5, 40 mM KCl, 10 mM MgCl2, at 37C
12256
PDB
SCOP
CATH
ORGANISM
Agrobacterium tumefaciens (strain C58 / ATCC 33970)
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystals are grown by the hanging drop vapor diffusion method; crystal structure of the enzyme with ADP reveals a novel nucleotide binding fold. The N-terminal domain contains an unusual left-handed beta,alpha,beta unit, while the C-terminal domain has a central alpha-beta plait fold with an insertion of four helices
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crystals are grown by the hanging drop vapor diffusion method; the enzyme ternary complexes with its amino acid substrate and ATP analogues determined by X-ray crystallography
Q58504
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
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expression of Escherichia coli homoserine kinase in Solanum tuberosum plants 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
medicine
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potential target for antibiotics due to the fact, that the pathway is not found in mammals