Literature summary for 2.6.1.32 extracted from

Yoneyama, H.; Hori, H.; Lim, S.J.; Murata, T.; Ando, T.; Isogai, E.; Katsumata, R.
Isolation of a mutant auxotrophic for L-alanine and identification of three major aminotransferases that synthesize L-alanine in Escherichia coli (2011), Biosci. Biotechnol. Biochem., 75, 930-938.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli	D2AFZ3	-	-

Synonyms

Synonyms	Comment	Organism
YfbQ	a novel aminotransferase	Escherichia coli
YfdZ	uncharacterized aminotransferase	Escherichia coli

Expression

Organism	Comment	Expression
Escherichia coli	level of yfdZ expression in minimal medium is higher than in rich medium	up

General Information

General Information	Comment	Organism
physiological function	an alanine auxotroph (mutated in yfdZ) is isolated from a prototrophic double mutant deficient in AvtA and YfbQ by chemical mutagenesis; Escherichia coli synthesizes L-alanine by means of three aminotransferases, YfbQ, YfdZ, and AvtA; YfbQ contributes to most of the alanine aminotransferase activity in rich medium	Escherichia coli
physiological function	an alanine auxotroph (mutated in yfdZ) is isolated from a prototrophic double mutant deficient in AvtA and YfbQ, a novel alanine aminotransferase, by chemical mutagenesis; Escherichia coli synthesizes L-alanine by means of three aminotransferases, YfbQ, YfdZ, and AvtA; level of yfdZ expression in minimal medium is higher than in rich medium	Escherichia coli

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Release 2023.1 (January 2023)