Information on EC 2.6.1.70 - aspartate-phenylpyruvate transaminase

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The expected taxonomic range for this enzyme is: Pseudomonas putida

EC NUMBER
COMMENTARY
2.6.1.70
-
RECOMMENDED NAME
GeneOntology No.
aspartate-phenylpyruvate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-aspartate + phenylpyruvate = oxaloacetate + L-phenylalanine
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate:phenylpyruvate aminotransferase
The enzyme from Pseudomonas putida also acts on 4-hydroxy-phenylpyruvate and, more slowly, on L-glutamate and L-histidine.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aspartate-phenylpyruvate aminotransferase
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-
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CAS REGISTRY NUMBER
COMMENTARY
99533-45-6
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-aspartate
L-glutamate + oxaloaspartate
show the reaction diagram
-
34% activity with respect to L-phenylpyruvate
-
-
?
2-oxoglutarate + L-phenylalanine
L-glutamate + L-phenylpyruvate
show the reaction diagram
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reverse reaction, 31% activity with respect to oxalacetate
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-
r
2-oxoisovalerate + L-aspartate
L-norvaline + oxaloacetate
show the reaction diagram
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6% activity with respect to L-phenylpyruvate
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-
?
2-oxoisovalerate + L-phenylalanine
L-norvaline + L-phenylpyruvate
show the reaction diagram
-
reverse reaction, 8% activity with respect to oxalacetate
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-
r
beta-methyl-DL-aspartate + phenyl 2-oxopropanoate
3-methyl-2-oxobutanedioate + L-phenylalanine
show the reaction diagram
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2% activity with respect to L-aspartate
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-
?
DL-p-fluorophenylalanine + oxaloacetate
p-fluorophenylpyruvate + L-aspartate
show the reaction diagram
-
reverse reaction, 51% activity with respect to L-phenylalanine
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-
r
indolepyruvate + L-aspartate
oxaloaspartate + L-tryptophan
show the reaction diagram
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10% activity with respect to L-phenylpyruvate
-
-
?
L-aspartate + phenyl 2-oxopropanoate
oxaloacetate + L-phenylalanine
show the reaction diagram
-
-
oxaloacetate decomposition drives the reaction towards L-phenylalanine
r
L-tryptophan + oxaloacetate
3-indole-2-oxopropanoate + L-aspartate
show the reaction diagram
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reverse reaction, 77% activity with respect to L-phenylalanine
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-
r
oxaloacetate + L-histidine
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-aspartate
show the reaction diagram
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reverse reaction, 4% activity with respect to L-phenylalanine
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r
oxaloacetate + L-tyrosine
p-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
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reverse reaction, 38% activity with respect to L-phenylalanine
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r
p-hydroxyphenylpyruvate + L-aspartate
oxaloacetate + L-tyrosine
show the reaction diagram
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54% activity with respect to L-phenylpyruvate
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-
?
p-hydroxyphenylpyruvate + L-phenylalanine
L-tyrosine + L-phenylpyruvate
show the reaction diagram
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reverse reaction, 52% activity with respect to oxalacetate
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-
r
phenyl 2-oxopropanoate + L-histidine
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-phenylalanine
show the reaction diagram
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4% activity with respect to L-aspartate
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-
?
phenyl 2-oxopropanoate + L-tyrosine
p-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
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27% activity with respect to aspartate
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-
?
L-tryptophan + phenyl 2-oxopropanoate
3-indole-2-oxopropanoate + L-phenylalanine
show the reaction diagram
-
40% activity with respect to aspartate
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-
?
additional information
?
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cysteine, glutamine, arginine, alanine, threonine, L-aspartate dibutylester, L-phenylglycine, isoleucine, valine, serine, lysine, ketobutyrate, alpha-keto-beta-n-valerate, beta-hydroxypyruvate, prephenate are inert as substrates, D amino acids are not utilized as substrates, modification of the carboxyl group of L-phenylalanine exhibits great influence on the enzyme substrate interaction as do substituents at C-2 or shortening the side chain, aspartate derivatives are used only with low activity if a modification at the position of the beta carbon is made, addition of substituents in the aromatic ring in the para position decreases the affinity of the derivative to the enzyme apparently with increasing bulk of the group, for a given halogen, position at the aromatic ring has only marginal influence on the reaction rate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate + phenyl 2-oxopropanoate
oxaloacetate + L-phenylalanine
show the reaction diagram
-
-
oxaloacetate decomposition drives the reaction towards L-phenylalanine
r
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CoCl2
-
retains 35% activity at 10 mM
EDTA
-
complete inhibition at 10 mM
HgCl2
-
irreversible and complete inhibition is observed at concentrations about 0.1 mM
KCN
-
irreversible inhibitor
MnCl2
-
retains 65% activity at 10 mM
p-chloromercuribenzoate
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irreversible and complete inhibition is observed at concentrations about 0.1 mM
phenyl 2-oxopropanoate
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phenylhydrazine
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irreversible inhibitor; retains 56% activity at 0.01 mM, retains 18% activity at 0.1 mM
pyridoxal 5'-phosphate
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at concentrations higher than 0.05 mM inhibitory effects are observed
Semicarbazide
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irreversible inhibitor; retains 59% activity at 0.01 mM, retains 24% activity at 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
the addition to the reaction mixture immediately before carrying out the enzymatic assay has no influence on activity, but preincubation increases the activity about twofold; the optimum of activation is obtained with a 0.05 mM concentration
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
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assay at
55
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maximum reaction velocity is observed
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
72000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 36000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-18°C, 50% glycerol without loss of activity for over two years
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
centrifugation, DEAE-Sephacel and Sephacryl S-200
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centrifugation, streptomycin sulfate precipitation, several chromatographic steps and disc-gel electrophoresis
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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L-phenylalanine production as a building block of aspartame