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, 37°C
21
pyruvate
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cosubstrate L-histidine, pH 8.9, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13.8
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L-histidine with pyruvate, pH 8.9, 37°C
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
4°C, purified enzyme in 0.05 mM potassium phosphate buffer, pH 7.5, rapid inactivation
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4°C, 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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