Table 2 A summary of physical properties of residues affecting cold lability.
From: Conformational changes and loose packing promote E. coli Tryptophanase cold lability
Residue name | Volume (Ã…3) | Hydrophobicity[55] | Location | Comments |
|---|---|---|---|---|
Tyr74 | 193.6 | -1.3 | On the catalytic interface | Involved in hydrogen bonding with PLP and Arg103 from adjacent subunit |
Phe74 | 189.9 | 2.8 | On the catalytic interface | Â |
Trp330 | 227.8 | -0.9 | On the non-catalytic interface | Â |
Cys298 | 108.5 | 2.5 | Close to the catalytic interface | Oxidized with 2-mercaptoethanol |
Ser 298 | 89.0 | -0.8 | Close to the catalytic interface | Â |
Val15 | 140.0 | 4.2 | On the non-catalytic interface | Involved in inter subunit β-sheet network |
Ile16 | 166.7 | 4.5 | On the non-catalytic interface | Involved in inter subunit β-sheet network |
Met 57* | 162.9 | 1.9 | On the non-catalytic interface | Involved in inter subunit β-sheet network |