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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 (Å3) 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  
Trp330 227.8 -0.9 On the non-catalytic interface  
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  
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
  1. * Accordingly to P. Vulgaris numbering