Information on EC 2.6.1.58 - phenylalanine(histidine) transaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.58
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RECOMMENDED NAME
GeneOntology No.
phenylalanine(histidine) transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine + pyruvate = phenylpyruvate + L-alanine
show the reaction diagram
L-histidine and L-tyrosine can act instead of L-phenylalanine, in the reverse reaction, L-methionine, L-serine and L-glutamine can replace L-alanine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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L-histidine degradation V
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L-homophenylalanine biosynthesis
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L-phenylalanine degradation III
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L-tyrosine degradation III
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Metabolic pathways
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Phenylalanine metabolism
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Phenylalanine, tyrosine and tryptophan biosynthesis
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Tropane, piperidine and pyridine alkaloid biosynthesis
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Tyrosine metabolism
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histidine metabolism
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phenylalanine metabolism
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tyrosine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine:pyruvate aminotransferase
L-Histidine and L-tyrosine can act instead of L-phenylalanine; in the reverse reaction, L-methionine, L-serine and L-glutamine can replace L-alanine.
CAS REGISTRY NUMBER
COMMENTARY hide
72560-98-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
injection of glucagon elevates activity
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Manually annotated by BRENDA team
injection of glucagon elevates activity
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamine + phenylpyruvate
5-amino-2,5-dioxopentanoic acid + L-phenylalanine
show the reaction diagram
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?
L-histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
show the reaction diagram
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about 50% of activity compared to L-phenylalanine
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?
L-methionine + phenylpyruvate
4-methylsulfanyl-2-oxobutanoate + L-phenylalanine
show the reaction diagram
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?
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
show the reaction diagram
L-serine + phenylpyruvate
3-hydroxy-2-oxopropanoate + L-phenylalanine
show the reaction diagram
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?
L-tyrosine + pyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-alanine
show the reaction diagram
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about 27% of activity compared to L-phenylalanine
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additional information
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oxaloacetate and hydroxypyruvate may replace pyruvate as amino acceptor at lower rates, little or no activity with 2-oxoglutarate
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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
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
histidine
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10 mM: 56% inhibition with L-phenylalanine and pyruvate as substrates
hydroxylamine
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0.5 mM: 63% inhibition
Isonicotinic acid hydrazide
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2 mM: 27% inhibition
KCN
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1 mM: 22% inhibition
L-methionine
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10 mM: competitive inhibitor
p-chloromercuribenzoate
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0.25 mM: 48% inhibition, reactivation by addition of 2-mercaptoethanol
Semicarbazide
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1 mM: 12% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9
histidine
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cosubstrate pyruvate, pH 8.9, 37C
21
pyruvate
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cosubstrate L-histidine, pH 8.9, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13.8
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L-histidine with pyruvate, pH 8.9, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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mitochondrial fraction: 70% of enzymatic activity, cytosolic fraction: 12%
Manually annotated by BRENDA team
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mitochondrial fraction: 70% of enzymatic activity, cytosolic fraction: 12%
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000 - 81000
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gel filtration
75000 - 85000
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sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 38000-42000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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1 h, in 15 mM potassium phosphate buffer, pH 7.5: stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing, loss of most of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, purified enzyme in 0.05 mM potassium phosphate buffer, pH 7.5, rapid inactivation
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4C, purified enzyme in 50 mM potassium phosphate buffer, pH 7.5, stable for at least 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, isoelectric focusing of the purified enzyme results in detection of 4 forms with different pI, all forms are nearly identical with respect to physical and enzymatic properties, all forms are responsive to glucagon
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