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Literature summary extracted from

  • Ziehr, H.; Kula, M.R.
    Isolation and characterization of a highly inducible L-aspartate-phenylpyruvate transaminase from Pseudomonas putida (1985), J. Biotechnol., 3, 19-31.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.6.1.70 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 Pseudomonas putida
2.6.1.70 pyridoxal 5'-phosphate the optimum of activation is obtained with a 0.05 mM concentration Pseudomonas putida

Application

EC Number Application Comment Organism
2.6.1.70 synthesis L-phenylalanine production as a building block of aspartame Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.70 CoCl2 retains 35% activity at 10 mM Pseudomonas putida
2.6.1.70 EDTA complete inhibition at 10 mM Pseudomonas putida
2.6.1.70 HgCl2 irreversible and complete inhibition is observed at concentrations about 0.1 mM Pseudomonas putida
2.6.1.70 KCN irreversible inhibitor Pseudomonas putida
2.6.1.70 MnCl2 retains 65% activity at 10 mM Pseudomonas putida
2.6.1.70 p-chloromercuribenzoate irreversible and complete inhibition is observed at concentrations about 0.1 mM Pseudomonas putida
2.6.1.70 phenyl 2-oxopropanoate
-
Pseudomonas putida
2.6.1.70 phenylhydrazine irreversible inhibitor; retains 56% activity at 0.01 mM, retains 18% activity at 0.1 mM Pseudomonas putida
2.6.1.70 pyridoxal 5'-phosphate at concentrations higher than 0.05 mM inhibitory effects are observed Pseudomonas putida
2.6.1.70 Semicarbazide irreversible inhibitor; retains 59% activity at 0.01 mM, retains 24% activity at 0.1 mM Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.70 36000
-
2 * 36000, SDS-PAGE Pseudomonas putida
2.6.1.70 72000
-
gel filtration Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.70 L-aspartate + 3-phenylpyruvate Pseudomonas putida
-
oxaloacetate + L-phenylalanine oxaloacetate decomposition drives the reaction towards L-phenylalanine r

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.70 Pseudomonas putida
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.70 centrifugation, streptomycin sulfate precipitation, several chromatographic steps and disc-gel electrophoresis Pseudomonas putida

Storage Stability

EC Number Storage Stability Organism
2.6.1.70 -18°C, 50% glycerol without loss of activity for over two years Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.70 2-oxoglutarate + L-aspartate 34% activity with respect to L-phenylpyruvate Pseudomonas putida L-glutamate + oxaloaspartate
-
?
2.6.1.70 2-oxoglutarate + L-phenylalanine reverse reaction, 31% activity with respect to oxalacetate Pseudomonas putida L-glutamate + 3-phenylpyruvate
-
r
2.6.1.70 2-oxoisovalerate + L-aspartate 6% activity with respect to L-phenylpyruvate Pseudomonas putida L-norvaline + oxaloacetate
-
?
2.6.1.70 2-oxoisovalerate + L-phenylalanine reverse reaction, 8% activity with respect to oxalacetate Pseudomonas putida L-norvaline + 3-phenylpyruvate
-
r
2.6.1.70 3-phenylpyruvate + L-histidine 4% activity with respect to L-aspartate Pseudomonas putida 3-(1H-imidazol-4-yl)-2-oxopropanoate + L-phenylalanine
-
?
2.6.1.70 3-phenylpyruvate + L-tyrosine 27% activity with respect to aspartate Pseudomonas putida p-hydroxyphenylpyruvate + L-phenylalanine
-
?
2.6.1.70 beta-methyl-DL-aspartate + 3-phenylpyruvate 2% activity with respect to L-aspartate Pseudomonas putida 3-methyl-2-oxobutanedioate + L-phenylalanine
-
?
2.6.1.70 DL-p-fluorophenylalanine + oxaloacetate reverse reaction, 51% activity with respect to L-phenylalanine Pseudomonas putida p-fluorophenylpyruvate + L-aspartate
-
r
2.6.1.70 indolepyruvate + L-aspartate 10% activity with respect to L-phenylpyruvate Pseudomonas putida oxaloaspartate + L-tryptophan
-
?
2.6.1.70 L-aspartate + 3-phenylpyruvate
-
Pseudomonas putida oxaloacetate + L-phenylalanine oxaloacetate decomposition drives the reaction towards L-phenylalanine r
2.6.1.70 L-tryptophan + 3-phenylpyruvate 40% activity with respect to aspartate Pseudomonas putida 3-indole-2-oxopropanoate + L-phenylalanine
-
?
2.6.1.70 L-tryptophan + oxaloacetate reverse reaction, 77% activity with respect to L-phenylalanine Pseudomonas putida 3-indole-2-oxopropanoate + L-aspartate
-
r
2.6.1.70 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 Pseudomonas putida ?
-
?
2.6.1.70 additional information D amino acids are not utilized as substrates Pseudomonas putida ?
-
?
2.6.1.70 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 Pseudomonas putida ?
-
?
2.6.1.70 additional information aspartate derivatives are used only with low activity if a modification at the position of the beta carbon is made Pseudomonas putida ?
-
?
2.6.1.70 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 Pseudomonas putida ?
-
?
2.6.1.70 oxaloacetate + L-histidine reverse reaction, 4% activity with respect to L-phenylalanine Pseudomonas putida 3-(1H-imidazol-4-yl)-2-oxopropanoate + L-aspartate
-
r
2.6.1.70 oxaloacetate + L-tyrosine reverse reaction, 38% activity with respect to L-phenylalanine Pseudomonas putida p-hydroxyphenylpyruvate + L-aspartate
-
r
2.6.1.70 p-hydroxyphenylpyruvate + L-aspartate 54% activity with respect to L-phenylpyruvate Pseudomonas putida oxaloacetate + L-tyrosine
-
?
2.6.1.70 p-hydroxyphenylpyruvate + L-phenylalanine reverse reaction, 52% activity with respect to oxalacetate Pseudomonas putida L-tyrosine + 3-phenylpyruvate
-
r

Subunits

EC Number Subunits Comment Organism
2.6.1.70 dimer 2 * 36000, SDS-PAGE Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.70 30
-
assay at Pseudomonas putida
2.6.1.70 55
-
maximum reaction velocity is observed Pseudomonas putida

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.6.1.70 30 55
-
Pseudomonas putida