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Information on EC 2.6.1.9 - histidinol-phosphate transaminase and Organism(s) Escherichia coli and UniProt Accession P06986

for references in articles please use BRENDA:EC2.6.1.9
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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.9 histidinol-phosphate transaminase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Escherichia coli
UNIPROT: P06986
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
histidinol phosphate aminotransferase, histidinol-phosphate aminotransferase, hspat, hisc2, athpa1, imidazolylacetolphosphate aminotransferase, l-histidinol phosphate aminotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminotransferase, histidinol phosphate
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glutamic-imidazoleacetol phosphate transaminase
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HisC
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histidine:imidazoleacetol phosphate transaminase
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histidinol phosphate aminotransferase
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histidinol-phosphate aminotransferase
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IAP transaminase
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imidazoleacetol phosphate transaminase
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imidazolylacetolphosphate aminotransferase
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imidazolylacetolphosphate transaminase
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L-histidinol phosphate aminotransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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SYSTEMATIC NAME
IUBMB Comments
L-histidinol-phosphate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-98-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
L-histidinol phosphate + 2-oxoglutarate
show the reaction diagram
histidine pathway
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-
?
L-histidinol phosphate + 2-oxoglutarate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-Glu
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
L-histidinol phosphate + 2-oxoglutarate
show the reaction diagram
histidine pathway
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
dynamic light scattering experiments
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
native and complexed with L-histidinol phosphate or N-(5'-phosphopyridoxyl)-L-glutamate, hanging drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K214A
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increased pKa
N157A
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increased pKa
N157A/R335L
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increased pKa
R335L
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increased pKa
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Haruyama, K.; Nakai, T.; Miyahara, I.; Hirotsu, K.; Mizuguchi, H.; Hayashi, H.; Kagamiyama, H.
Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme
Biochemistry
40
4633-4644
2001
Escherichia coli (P06986), Escherichia coli
Manually annotated by BRENDA team
Mizuguchi, H.; Hayashi, H.; Miyahara, I.; Hirotsu, K.; Kagamiyama, H.
Characterization of histidinol phosphate aminotransferase from Escherichia coli
Biochim. Biophys. Acta
1647
321-324
2003
Escherichia coli
Manually annotated by BRENDA team
Sivaraman, J.; Li, Y.; Larocque, R.; Schrag, J.D.; Cygler, M.; Matte, A.
Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate
J. Mol. Biol.
311
761-776
2001
Escherichia coli (P06986), Escherichia coli
Manually annotated by BRENDA team