Table 5.
Conserved sequence patterns and catalytically active amino acids of AMDases and their function.
| Number | Sequence pattern | Function of conserved amino acids |
|---|---|---|
| (1) | GLIVPPAxGxVPxE(10-23) | Binding of aromatic residues |
| (2) | GLGLxxVxxxGY(37-48) | Destabilization of leaving carboxylic group |
| (3) | GAxxVxLMGTSLSFYRG(66-82) | G74 determines product’s stereoisomery; hydrogen bridge bond |
| (4) | RVAVxTAY(119-126) | Hydrogen bridge bond |
| (5) | LxIxxVxxV(151-159) | Destabilization of leaving carboxylic group |
| (6) | DALLISCGxL(182-191) | Active site Cys determines product’s stereoisomery, hydrogen bridge bond |
The letter x indicates an unconserved position within the sequence pattern. Numbering of amino acids is according to the AMDase from B. bronchiseptica KU1201. Catalytically active amino acids are printed in bold.