Protein Family Models

The D-amino acid transferases (D-AAT) are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity. Crystal structure. [1]. 7626635. Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Sugio S, Petsko GA, Manning JM, Soda K, Ringe D;. Biochemistry 1995;34:9661-9669. [2]. 9163511. Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution. Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H;. J Biochem 1997;121:637-641. (from Pfam)

Date:

2024-10-16

branched-chain-amino-acid transaminase catalyses the transamination of the branched-chain amino acids leucine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate

Date:

2023-03-16

Catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids

Date:

2021-07-22

Among the class IV aminotransferases are two phylogenetically separable groups of branched-chain amino acid aminotransferase (IlvE). The last common ancestor of the two lineages appears also to have given rise to a family of D-amino acid aminotransferases (DAAT). This model represents the IlvE family less similar to the DAAT family.

Gene:

ilvE

Date:

2024-06-10