Information on EC 2.6.1.9 - histidinol-phosphate transaminase

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

EC NUMBER
COMMENTARY hide
2.6.1.9
-
RECOMMENDED NAME
GeneOntology No.
histidinol-phosphate transaminase
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
histidine metabolism
-
-
Histidine metabolism
-
-
L-histidine biosynthesis
-
-
Metabolic pathways
-
-
Novobiocin biosynthesis
-
-
Phenylalanine metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
-
Tyrosine metabolism
-
-
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
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
L-tyrosine + 2-oxoglutarate
show the reaction diagram
-
-
-
?
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-2-aminoadipate
L-histidinol phosphate + 2-oxoadipate
show the reaction diagram
-
40% of the activity with L-glutamate
-
-
r
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-arginine
L-histidinol phosphate + 2-oxo-5-guanidinopentanoate
show the reaction diagram
-
33% of the activity with L-glutamate
-
-
r
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
L-histidinol phosphate + 2-oxoglutarate
show the reaction diagram
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamine
L-histidinol phosphate + 4-carbamoyl-2-oxobutanoate
show the reaction diagram
-
4% of the activity with L-glutamate
-
-
r
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-histidine
L-histidinol phosphate + 3-(1H-imidazol-4-yl)-2-oxopropanoate
show the reaction diagram
-
30% of the activity with L-glutamate
-
-
r
3-indole-2-oxopropanoate + L-glutamate
L-tryptophan + 2-oxoglutarate
show the reaction diagram
-
-
-
?
4-methyl-2-oxopentanoate + L-alanine
L-leucine + pyruvate
show the reaction diagram
-
-
-
?
4-methyl-2-oxopentanoate + L-asparagine
L-leucine + 2-oxosuccinamic acid
show the reaction diagram
-
-
-
?
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
show the reaction diagram
-
-
-
?
beta-chloro-L-alanine
pyruvate + NH3 + Cl-
show the reaction diagram
-
-
-
?
L-glutarate + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
show the reaction diagram
-
-
-
?
L-histidine + 2-oxoglutarate
3-(imidazol-4-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-histidinol phosphate + 2-oxo-5-guanidinopentanoate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-arginine
show the reaction diagram
-
-
-
-
r
L-histidinol phosphate + 2-oxoadipate
3-(imidazol-4-yl)-2-oxopropyl phosphate + 2-aminoadipate
show the reaction diagram
-
70% of the activity with 2-oxoglutarate
-
-
r
L-histidinol phosphate + 2-oxoglutarate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-Glu
show the reaction diagram
L-histidinol phosphate + 2-oxoglutarate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
show the reaction diagram
L-histidinol phosphate + 4-hydroxyphenylpyruvate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-tyrosine
show the reaction diagram
-
-
-
-
?
L-histidinol phosphate + oxaloacetate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-aspartate
show the reaction diagram
-
-
-
-
?
L-histidinol phosphate + phenylpyruvate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
L-histidinol phosphate + pyruvate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-Ala
show the reaction diagram
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
r
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
L-histidinol phosphate + 2-oxoglutarate
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
show the reaction diagram
Q9X0D0
catalytic reaction pathway, histidine biosynthesis
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-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
0.004 M, 80% inhibition
Cu2+
-
0.004 M, 80% inhibition
hydroxylamine
-
0.004 M, 80% inhibition
iodoacetate
-
0.004 M, 95% inhibition
L-glutamate
-
competitive to tyrosine
Semicarbazide
-
0.004 M, 80% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
omega-Methylpyridoxal phosphate
-
can replace pyridoxal phosphate, Km: 0.004 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 7.1
2-oxoglutarate
0.15 - 9.1
L-Histidinol phosphate
32.8 - 94.9
L-leucine
2.5 - 106
L-phenylalanine
3.4
L-tryptophan
pH 8.0, 20C
0.71 - 2.3
L-tyrosine
43.48
phenylalanine
-
pH 7, 37C
3.39
tyrosine
-
pH 7, 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046 - 1.93
L-Histidinol phosphate
0.66 - 3.27
L-leucine
0.009 - 4.1
L-phenylalanine
0.014
L-tryptophan
Thermotoga maritima
Q9X0D0
pH 8.0, 25C
0.043
L-tyrosine
Thermotoga maritima
Q9X0D0
pH 8.0, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01266
protein extract after expression in wild-type Escherichia coli DH5alpha
0.1
substrates 4-methyl-2-oxopentanoate, L-alanine
0.2
substrates L-glutarate, 2-oxobutanoate
0.3
substrates 3-indole-2-oxopropanoate, L-glutamate
0.4
substrates 4-methyl-2-oxopentanoate, L-asparagine
0.5
substrates 3-(4-hydroxyphenyl)-2-oxopropanoate, L-glutamate
1.4
substrates 4-methyl-2-oxopentanoate, L-glutamate
1.5
substrates phenylpyruvate, L-glutamate
2.8
substrates L-histidinol phosphate, 2-oxoglutarate
7
-
2-oxoglutarate + histidinol-phosphate
7.11
-
4-hydroxyphenylpyruvate + histidinol-phosphate
11.6
-
2-oxoglutarate + phenylalanine; 2-oxoglutarate + tyrosine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1
-
diphosphate buffer
8.4
-
diethanolamine buffer
8.5
-
triethanolamine buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
-
pH 7.5: about 85% of activity maximum, pH 9.0: about 50% of activity maximum, diphosphate buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Listeria innocua serovar 6a (strain CLIP 11262)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Rhizobium meliloti (strain 1021)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
gel filtration
45400
calculated from nucleotide sequence
59000
-
equilibrium centrifugation, pyridoxal phosphate analysis, spectrophotometric assay, phosphate analysis, viscometry
60000
-
dynamic light scattering experiments
74000
-
sedimentation equilibrium measurement
85000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
marked tendency to polymerize upon ageing
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo histidinol-phosphate aminotransferase the internal PLP aldimine adduct and a pyridoxamine 5'-phosphate enzyme complex at resolutions of 2.2 A, 2.1 A and 1.8 A, respectively. The hydrogen bond between the side chain of residue Y21 and the phosphate group of histidinol phosphate is important for recognition of the natural substrate and discrimination against other potential amino donors. Residue N99 does not contribute to the specific recognition of the amino-acid donor. Residues Y123 and Y257 interact with the substrate through van der Waals-interactions
hanging drop vapor diffusion method
-
native and complexed with L-histidinol phosphate or N-(5'-phosphopyridoxyl)-L-glutamate, hanging drop vapor diffusion method
-
diffraction-quality crystals are grown using the hanging-drop vapour-diffusion technique. X-ray diffraction data are recorded to 2.45 A resolution
-
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, 20C, 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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
stable overnight
636659
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
holoenzyme and apoenzyme are stable for 15 min
45
-
holoenzyme loses 15% activity after 5 min, apoenzyme loses 70% activity after 5 min
50
-
no loss of activity for 2 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C over night and thawing on ice: 98% loss of activity
-
-20C, stable for several months
-
-80C no loss of activity after several months when stored in 10% glycerol
-
-80C over night and thawing on ice: 58% loss of activity
-
0C, 1 month, 30% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C141-T1710, C141
-
from derepressed histidine auxotrophs, 95% pure
-
purified to homogeneity using nickel-nitrilotriacetic acid metal-affinity and gel filtration chromatography
-
recombinant protein
-
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) and B834(DE3), respectively
use of omega-aminoalkylagaroses, 15fold purification in one step
-
wild-type and mutant enzymes
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain BL21(DE3) and B834(DE3), respectively
HisC2 is overexpressed in Mycobacterium smegmatis
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N99D
6fold reduction in ratio kcat to Km for substrates L-histidinol phosphate, 2-oxoglutarate
Y123F
4fold reduction in ratio kcat to Km for substrates L-histidinol phosphate, 2-oxoglutarate
Y21F
10fold reduction in ratio kcat to Km for substrates L-histidinol phosphate, 2-oxoglutarate
Y257F
5fold reduction in ratio kcat to Km for substrates L-histidinol phosphate, 2-oxoglutarate
K214A
-
increased pKa
N157A
-
increased pKa
N157A/R335L
-
increased pKa
R335L
-
increased pKa
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
holoenzyme and apoenzyme can be constituted in vitro with pyridoxal 5'-phosphate
-
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