1daa
From Proteopedia
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CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE
Overview
The three-dimensional structure of D-amino acid aminotransferase (D-AAT), in the pyridoxamine phosphate form has been determined, crystallographically. The fold of this pyridoxal phosphate, (PLP)-containing enzyme is completely different from those of any of the, other enzymes that utilize PLP as part of their mechanism and whose, structures are known. However, there are some striking similarities, between the active sites of D-AAT and the corresponding enzyme that, transaminates L-amino acids, L-aspartate aminotransferase. These, similarities represent convergent evolution to a common solution of the, problem of enforcing transamination chemistry on the PLP cofactor., Implications of these similarities are discussed in terms of their, possible roles in the stabilization of intermediates of a transamination, reaction. In addition, sequence similarity between D-AAT and branched, chain L-amino acid aminotransferase suggests that this latter enzyme will, also have a fold similar to that of D-AAT.
About this Structure
1DAA is a Single protein structure of sequence from Bacillus sp. with PLP as ligand. Active as D-amino-acid transaminase, with EC number 2.6.1.21 Full crystallographic information is available from OCA.
Reference
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 Aug 1;34(30):9661-9. PMID:7626635
Page seeded by OCA on Tue Nov 20 13:07:02 2007
