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Literature summary extracted from

  • Jhee, K.H.; Yoshimura, T.; Miles, E.W.; Takeda, S.; Miyahara, I.; Hirotsu, K.; Soda, K.; Kawata, Y.; Esaki, N.
    Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry (2000), J. Biochem., 128, 679-686.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.38 expression in Escherichia coli JM109 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.3.38 D-alanine + pyridoxal 5'-phosphate Escherichia coli L-alanine and other D- and L-amino acids tested are inert as substrates of transamination pyridoxamine 5'-phosphate + pyruvate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.38 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.38 fractionation with ammonium sulfate pH 7.5, DEAE-Sephacel column, butyl-Sepharose 4B column, Gigapite column Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.38 4-amino-4-deoxychorismate
-
 Escherichia coli 4-aminobenzoate + pyruvate
-
 ?
4.1.3.38 D-alanine + pyridoxal 5'-phosphate L-alanine and other D- and L-amino acids tested are inert as substrates of transamination Escherichia coli pyridoxamine 5'-phosphate + pyruvate
-
 r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.3.38 30
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.3.38 pyridoxal 5'-phosphate
-
 Escherichia coli