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aminotransferase class IV
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)
branched-chain amino acid transaminase
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
branched-chain amino acid aminotransferase
Catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids
branched-chain-amino-acid transaminase
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.
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