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Information on EC 2.6.1.9 - histidinol-phosphate transaminase and Organism(s) Thermotoga maritima and UniProt Accession Q9X0D0

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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:
Thermotoga maritima
UNIPROT: Q9X0D0
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The taxonomic range for the selected organisms is: Thermotoga maritima
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
histidinol-phosphate aminotransferase
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aminotransferase, histidinol phosphate
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-
-
-
glutamic-imidazoleacetol phosphate transaminase
-
-
-
-
HisC
-
-
-
-
histidine:imidazoleacetol phosphate transaminase
-
-
-
-
histidinol phosphate aminotransferase
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-
-
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histidinol-phosphate aminotransferase
-
-
-
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IAP transaminase
-
-
-
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imidazoleacetol phosphate transaminase
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-
-
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imidazolylacetolphosphate aminotransferase
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-
-
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imidazolylacetolphosphate transaminase
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-
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L-histidinol phosphate aminotransferase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
show the reaction diagram
mechanism via gem-diamino, aldimine, and ketimine reaction intermediates, active site structure analysis, overview
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-histidinol phosphate + 2-oxoglutarate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
show the reaction diagram
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
low activity with
-
-
r
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
r
additional information
?
-
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
L-histidinol phosphate + 2-oxoglutarate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
show the reaction diagram
catalytic reaction pathway, histidine biosynthesis
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-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
covalently bound
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
L-histidinol phosphate
pH 8.0, 20°C
38
L-phenylalanine
pH 8.0, 20°C
3.4
L-tryptophan
pH 8.0, 20°C
2.3
L-tyrosine
pH 8.0, 20°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046
L-histidinol phosphate
pH 8.0, 25°C
0.009
L-phenylalanine
pH 8.0, 25°C
0.014
L-tryptophan
pH 8.0, 25°C
0.043
L-tyrosine
pH 8.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene tmHspAT
Swissprot
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and selenomethionine-labeled enzyme, with or without bound pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate, sitting drop vapour diffusion method, 0.001 ml equal volumes of protein and reservoir solutions, 20°C, 50% v/v ethylene glycol, 5% w/v PEG 1000, sodium acetate, pH 5.1, 2-3 weeks, X-ray diffraction structure determination and analysis at 3.5 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) and B834(DE3), respectively
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain BL21(DE3) and B834(DE3), respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fernandez, F.J.; Vega, M.C.; Lehmann, F.; Sandmeier, E.; Gehring, H.; Christen, P.; Wilmanns, M.
Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase
J. Biol. Chem.
279
21478-21488
2004
Thermotoga maritima (Q9X0D0), Thermotoga maritima
Manually annotated by BRENDA team