Literature summary for 2.6.1.1 extracted from

Hayashi, H.; Mizuguchi, H.; Miyahara, I.; Nakajima, Y.; Hirotsu, K.; Kagamiyama, H.
Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis (2003), J. Biol. Chem., 278, 9481-9488.

Search for more literature for 2.6.1.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of V39F AspAT is performed by the hanging drop vapor diffusion method	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
V39F	mutant enzyme shows a more open conformation, and the aldimine pKa is lowered by 0.7 unit compared with the wild-type enzyme. The maleate-bound V39F enzyme shows the aldimine pKa 0.9 unit lower than that of the maleate-bound wild-type enzyme. The maleate-bound V39F enzyme shows an altered side-chain packing pattern in the 3739 region, and the lack of repulsion between Gly38 carbonyl O and Tyr225 seems to be the cause of the reduced pKa value	Escherichia coli
V39F/N194A	mutation does not decrease the aldimine pKa, showing that the domain rotation controls the aldimine pKa via the Arg386-Asn194 pyridoxal 5'-phosphate linkage system	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00509	-	-

Synonyms

Synonyms	Comment	Organism
aspartate, 2-oxoglutarate aminotransferase	-	Escherichia coli
AspAT	-	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)