Literature summary for 4.1.3.38 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli JM109	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-amino-4-deoxychorismate	-	Escherichia coli	4-aminobenzoate + pyruvate	-	?
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]

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

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Escherichia coli

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Release 2023.1 (January 2023)