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A positively charged amino acid at position 129 in nitrilase from Rhodococcus rhodochrous ATCC 33278 is an essential residue for the activity with meta ‐substituted benzonitriles
Author(s) -
Yeom Soo-Jin,
Lee Jung-Kul,
Oh Deok-Kun
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.11.008
Subject(s) - nitrilase , rhodococcus rhodochrous , chemistry , steric effects , substituent , residue (chemistry) , stereochemistry , enzyme , rhodococcus , amino acid , mutant , biochemistry , gene
A positively charged amino acid (Arg, Lys, or His) at position 129 in Rhodococcus rhodochrous ATCC 33278 nitrilase is essential for the activity of aromatic nitriles. The wild‐type enzyme containing Arg129 was active only for meta ‐ and para ‐substituted benzonitriles with a methyl or amino group, but the R129K and R129H mutant enzymes were active only for meta ‐substituted benzonitriles. The lack of activity of the mutants for para ‐substituted benzonitriles may be attributable to steric hindrance between the para ‐substituent and the side chain of Lys or His.