BRENDA - Enzyme Database show
show all sequences of 2.6.1.70

Isolation and characterization of a highly inducible L-aspartate-phenylpyruvate transaminase from Pseudomonas putida

Ziehr, H.; Kula, M.R.; J. Biotechnol. 3, 19-31 (1985)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
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
Pseudomonas putida
Application
Application
Commentary
Organism
synthesis
L-phenylalanine production as a building block of aspartame
Pseudomonas putida
Inhibitors
Inhibitors
Commentary
Organism
Structure
CoCl2
retains 35% activity at 10 mM
Pseudomonas putida
EDTA
complete inhibition at 10 mM
Pseudomonas putida
HgCl2
irreversible and complete inhibition is observed at concentrations about 0.1 mM
Pseudomonas putida
KCN
irreversible inhibitor
Pseudomonas putida
MnCl2
retains 65% activity at 10 mM
Pseudomonas putida
p-chloromercuribenzoate
irreversible and complete inhibition is observed at concentrations about 0.1 mM
Pseudomonas putida
phenyl 2-oxopropanoate
-
Pseudomonas putida
phenylhydrazine
irreversible inhibitor; retains 56% activity at 0.01 mM, retains 18% activity at 0.1 mM
Pseudomonas putida
pyridoxal 5'-phosphate
at concentrations higher than 0.05 mM inhibitory effects are observed
Pseudomonas putida
Semicarbazide
irreversible inhibitor; retains 59% activity at 0.01 mM, retains 24% activity at 0.1 mM
Pseudomonas putida
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
2 * 36000, SDS-PAGE
Pseudomonas putida
72000
-
gel filtration
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-aspartate + 3-phenylpyruvate
Pseudomonas putida
-
oxaloacetate + L-phenylalanine
oxaloacetate decomposition drives the reaction towards L-phenylalanine
Pseudomonas putida
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Purification (Commentary)
Commentary
Organism
centrifugation, streptomycin sulfate precipitation, several chromatographic steps and disc-gel electrophoresis
Pseudomonas putida
Storage Stability
Storage Stability
Organism
-18C, 50% glycerol without loss of activity for over two years
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxoglutarate + L-aspartate
34% activity with respect to L-phenylpyruvate
640191
Pseudomonas putida
L-glutamate + oxaloaspartate
-
-
-
?
2-oxoglutarate + L-phenylalanine
reverse reaction, 31% activity with respect to oxalacetate
640191
Pseudomonas putida
L-glutamate + 3-phenylpyruvate
-
-
-
r
2-oxoisovalerate + L-aspartate
6% activity with respect to L-phenylpyruvate
640191
Pseudomonas putida
L-norvaline + oxaloacetate
-
-
-
?
2-oxoisovalerate + L-phenylalanine
reverse reaction, 8% activity with respect to oxalacetate
640191
Pseudomonas putida
L-norvaline + 3-phenylpyruvate
-
-
-
r
3-phenylpyruvate + L-histidine
4% activity with respect to L-aspartate
640191
Pseudomonas putida
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-phenylalanine
-
-
-
?
3-phenylpyruvate + L-tyrosine
27% activity with respect to aspartate
640191
Pseudomonas putida
p-hydroxyphenylpyruvate + L-phenylalanine
-
-
-
?
beta-methyl-DL-aspartate + 3-phenylpyruvate
2% activity with respect to L-aspartate
640191
Pseudomonas putida
3-methyl-2-oxobutanedioate + L-phenylalanine
-
-
-
?
DL-p-fluorophenylalanine + oxaloacetate
reverse reaction, 51% activity with respect to L-phenylalanine
640191
Pseudomonas putida
p-fluorophenylpyruvate + L-aspartate
-
-
-
r
indolepyruvate + L-aspartate
10% activity with respect to L-phenylpyruvate
640191
Pseudomonas putida
oxaloaspartate + L-tryptophan
-
-
-
?
L-aspartate + 3-phenylpyruvate
-
640191
Pseudomonas putida
oxaloacetate + L-phenylalanine
oxaloacetate decomposition drives the reaction towards L-phenylalanine
640191
Pseudomonas putida
r
L-tryptophan + 3-phenylpyruvate
40% activity with respect to aspartate
640191
Pseudomonas putida
3-indole-2-oxopropanoate + L-phenylalanine
-
-
-
?
L-tryptophan + oxaloacetate
reverse reaction, 77% activity with respect to L-phenylalanine
640191
Pseudomonas putida
3-indole-2-oxopropanoate + L-aspartate
-
-
-
r
additional information
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
640191
Pseudomonas putida
?
-
-
-
-
additional information
D amino acids are not utilized as substrates
640191
Pseudomonas putida
?
-
-
-
-
additional information
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
640191
Pseudomonas putida
?
-
-
-
-
additional information
aspartate derivatives are used only with low activity if a modification at the position of the beta carbon is made
640191
Pseudomonas putida
?
-
-
-
-
additional information
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
640191
Pseudomonas putida
?
-
-
-
-
oxaloacetate + L-histidine
reverse reaction, 4% activity with respect to L-phenylalanine
640191
Pseudomonas putida
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-aspartate
-
-
-
r
oxaloacetate + L-tyrosine
reverse reaction, 38% activity with respect to L-phenylalanine
640191
Pseudomonas putida
p-hydroxyphenylpyruvate + L-aspartate
-
-
-
r
p-hydroxyphenylpyruvate + L-aspartate
54% activity with respect to L-phenylpyruvate
640191
Pseudomonas putida
oxaloacetate + L-tyrosine
-
-
-
?
p-hydroxyphenylpyruvate + L-phenylalanine
reverse reaction, 52% activity with respect to oxalacetate
640191
Pseudomonas putida
L-tyrosine + 3-phenylpyruvate
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer
2 * 36000, SDS-PAGE
Pseudomonas putida
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Pseudomonas putida
55
-
maximum reaction velocity is observed
Pseudomonas putida
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
30
55
-
Pseudomonas putida
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
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
Pseudomonas putida
Application (protein specific)
Application
Commentary
Organism
synthesis
L-phenylalanine production as a building block of aspartame
Pseudomonas putida
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CoCl2
retains 35% activity at 10 mM
Pseudomonas putida
EDTA
complete inhibition at 10 mM
Pseudomonas putida
HgCl2
irreversible and complete inhibition is observed at concentrations about 0.1 mM
Pseudomonas putida
KCN
irreversible inhibitor
Pseudomonas putida
MnCl2
retains 65% activity at 10 mM
Pseudomonas putida
p-chloromercuribenzoate
irreversible and complete inhibition is observed at concentrations about 0.1 mM
Pseudomonas putida
phenyl 2-oxopropanoate
-
Pseudomonas putida
phenylhydrazine
irreversible inhibitor; retains 56% activity at 0.01 mM, retains 18% activity at 0.1 mM
Pseudomonas putida
pyridoxal 5'-phosphate
at concentrations higher than 0.05 mM inhibitory effects are observed
Pseudomonas putida
Semicarbazide
irreversible inhibitor; retains 59% activity at 0.01 mM, retains 24% activity at 0.1 mM
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
2 * 36000, SDS-PAGE
Pseudomonas putida
72000
-
gel filtration
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-aspartate + 3-phenylpyruvate
Pseudomonas putida
-
oxaloacetate + L-phenylalanine
oxaloacetate decomposition drives the reaction towards L-phenylalanine
Pseudomonas putida
r
Purification (Commentary) (protein specific)
Commentary
Organism
centrifugation, streptomycin sulfate precipitation, several chromatographic steps and disc-gel electrophoresis
Pseudomonas putida
Storage Stability (protein specific)
Storage Stability
Organism
-18C, 50% glycerol without loss of activity for over two years
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxoglutarate + L-aspartate
34% activity with respect to L-phenylpyruvate
640191
Pseudomonas putida
L-glutamate + oxaloaspartate
-
-
-
?
2-oxoglutarate + L-phenylalanine
reverse reaction, 31% activity with respect to oxalacetate
640191
Pseudomonas putida
L-glutamate + 3-phenylpyruvate
-
-
-
r
2-oxoisovalerate + L-aspartate
6% activity with respect to L-phenylpyruvate
640191
Pseudomonas putida
L-norvaline + oxaloacetate
-
-
-
?
2-oxoisovalerate + L-phenylalanine
reverse reaction, 8% activity with respect to oxalacetate
640191
Pseudomonas putida
L-norvaline + 3-phenylpyruvate
-
-
-
r
3-phenylpyruvate + L-histidine
4% activity with respect to L-aspartate
640191
Pseudomonas putida
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-phenylalanine
-
-
-
?
3-phenylpyruvate + L-tyrosine
27% activity with respect to aspartate
640191
Pseudomonas putida
p-hydroxyphenylpyruvate + L-phenylalanine
-
-
-
?
beta-methyl-DL-aspartate + 3-phenylpyruvate
2% activity with respect to L-aspartate
640191
Pseudomonas putida
3-methyl-2-oxobutanedioate + L-phenylalanine
-
-
-
?
DL-p-fluorophenylalanine + oxaloacetate
reverse reaction, 51% activity with respect to L-phenylalanine
640191
Pseudomonas putida
p-fluorophenylpyruvate + L-aspartate
-
-
-
r
indolepyruvate + L-aspartate
10% activity with respect to L-phenylpyruvate
640191
Pseudomonas putida
oxaloaspartate + L-tryptophan
-
-
-
?
L-aspartate + 3-phenylpyruvate
-
640191
Pseudomonas putida
oxaloacetate + L-phenylalanine
oxaloacetate decomposition drives the reaction towards L-phenylalanine
640191
Pseudomonas putida
r
L-tryptophan + 3-phenylpyruvate
40% activity with respect to aspartate
640191
Pseudomonas putida
3-indole-2-oxopropanoate + L-phenylalanine
-
-
-
?
L-tryptophan + oxaloacetate
reverse reaction, 77% activity with respect to L-phenylalanine
640191
Pseudomonas putida
3-indole-2-oxopropanoate + L-aspartate
-
-
-
r
additional information
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
640191
Pseudomonas putida
?
-
-
-
-
additional information
D amino acids are not utilized as substrates
640191
Pseudomonas putida
?
-
-
-
-
additional information
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
640191
Pseudomonas putida
?
-
-
-
-
additional information
aspartate derivatives are used only with low activity if a modification at the position of the beta carbon is made
640191
Pseudomonas putida
?
-
-
-
-
additional information
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
640191
Pseudomonas putida
?
-
-
-
-
oxaloacetate + L-histidine
reverse reaction, 4% activity with respect to L-phenylalanine
640191
Pseudomonas putida
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-aspartate
-
-
-
r
oxaloacetate + L-tyrosine
reverse reaction, 38% activity with respect to L-phenylalanine
640191
Pseudomonas putida
p-hydroxyphenylpyruvate + L-aspartate
-
-
-
r
p-hydroxyphenylpyruvate + L-aspartate
54% activity with respect to L-phenylpyruvate
640191
Pseudomonas putida
oxaloacetate + L-tyrosine
-
-
-
?
p-hydroxyphenylpyruvate + L-phenylalanine
reverse reaction, 52% activity with respect to oxalacetate
640191
Pseudomonas putida
L-tyrosine + 3-phenylpyruvate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 36000, SDS-PAGE
Pseudomonas putida
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Pseudomonas putida
55
-
maximum reaction velocity is observed
Pseudomonas putida
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
30
55
-
Pseudomonas putida
Other publictions for EC 2.6.1.70
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
640192
Ziehr
-
Continuous production of L-phe ...
Pseudomonas putida
Biotechnol. Bioeng.
XXIX
482-487
1987
-
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1
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1
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1
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1
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640191
Ziehr
-
Isolation and characterization ...
Pseudomonas putida
J. Biotechnol.
3
19-31
1985
1
1
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10
-
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2
1
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1
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1
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21
1
2
1
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1
1
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10
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1
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1
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21
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1
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