Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.1.39 - homoserine kinase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58504

for references in articles please use BRENDA:EC2.7.1.39
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Methanocaldococcus jannaschii
UNIPROT: Q58504 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hsk, homoserine kinase, thr1p, atp:l-homoserine o-phosphotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homoserine kinase
-
-
homoserine kinase (phosphorylating)
-
-
-
-
HSK
-
-
-
-
kinase (phosphorylating), homoserine
-
-
-
-
kinase, homoserine (phosphorylating)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:L-homoserine O-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-58-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-homoserine
ADP + O-phospho-L-homoserine
show the reaction diagram
ATP + L-homoserine
ADP + O-phospho-L-homoserine
show the reaction diagram
L-homoserine + ATP
O-phospho-L-homoserine + ADP
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-homoserine
ADP + O-phospho-L-homoserine
show the reaction diagram
fourth enzyme in the aspartate pathway of amino acid biosynthesis
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
ATP
-
method: isothermal titration calometry
0.087
L-homoserine
-
method: isothermal titration calometry
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.75
L-homoserine
-
method: isothermal titration calometry
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
crystals are grown by the hanging drop vapor diffusion method
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, T.; Daugherty, M.; Grishin, N.V.; Osterman, A.L.; Zhang, H.
Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily
Structure Fold. Des.
8
1247-1257
2000
Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Krishna, S.S.; Zhou, T.; Daugherty, M.; Osterman, A.; Zhang, H.
Structural basis for the catalysis and substrate specificity of homoserine kinase
Biochemistry
40
10810-10818
2001
Methanocaldococcus jannaschii (Q58504), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Stockbridge, R.B.; Wolfenden, R.
The intrinsic reactivity of ATP and the catalytic proficiencies of kinases acting on glucose, N-acetylgalactosamine, and homoserine: a thermodynamic analysis
J. Biol. Chem.
284
22747-22757
2009
Methanocaldococcus jannaschii
Manually annotated by BRENDA team