Article
Reversible dissociation/association of D-amino acid transaminase subunits: properties of isolated active dimers and inactive monomers.
Biochemistry - 18 Jan 2000
Kishimoto K, Yasuda C, Manning J M
Abstract excerpt
The crystal structure of dimeric D-amino acid transaminase shows that the two Trp-139 sites are located in a hydrophobic pocket at the interface between the subunits and that the two indole side chains face one another and are within 10 A of coenzyme. This enzyme prefers an aromatic character at position 139, as previously demonstrated by the finding that Phe-139 but no other substitution tested provides the...
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