Literature summary for 2.6.1.66 extracted from

Pena-Soler, E.; Fernandez, F.J.; Lopez-Estepa, M.; Garces, F.; Richardson, A.J.; Quintana, J.F.; Rudd, K.E.; Coll, M.; Vega, M.C.
Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli (2014), PLoS ONE, 9, e102139.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
homology modeling of structure and comparison with alanine transaminases AlaA and AlaC of Escherichia coli. The enzymes shared the same set of residues for binding the phosphate group and pyrimidine ring of the cofactor. Despite a high degree of sequence conservation in the active site, AvtA is thre least effective due to several changes in residues stabilizing the phosphate group and the secong half reaction	Escherichia coli

Crystallization (Comment)

Organism

homology modeling of structure and comparison with alanine transaminases AlaA and AlaC of Escherichia coli. The enzymes shared the same set of residues for binding the phosphate group and pyrimidine ring of the cofactor. Despite a high degree of sequence conservation in the active site, AvtA is thre least effective due to several changes in residues stabilizing the phosphate group and the secong half reaction

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09053	-	-

Synonyms

Synonyms	Comment	Organism
AvtA	-	Escherichia coli

Cofactor

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)