Dataset Information


Effect on catalysis by replacement of catalytic residue from hen egg white lysozyme to Venerupis philippinarum lysozyme.

ABSTRACT: Asn46Asp/Asp52Ser or Asn46Glu/Asp52Ser hen egg white lysozyme (HEL) mutant was designed by introducing the substituted catalytic residue Asp46 or Glu46, respectively, based on Venerupis philippinarum (Vp) lysozyme structure as a representative of invertebrate-type (i-type) lyzozyme. These mutations restored the bell-shaped pH-dependency of the enzyme activity from the sigmoidal pH-dependency observed for the Asp52Ser mutant. Furthermore both lysozyme mutants possessed retaining mechanisms like Vp lysozyme and HEL. The Asn46Glu/Asp52Ser mutant, which has a shorter distance between two catalytic residues, formed a glycosyl adduct in the reaction with the N-acetylglucosamine oligomer. Furthermore, we found the accelerated turnover through its glycosyl adduct formation and decomposition. The turnover rate estimated from the glycosyl formation and decomposition rates was only 20% of the observed hydrolysis rate of the substrate. Based on these results, we discussed the catalytic mechanism of lysozymes.


PROVIDER: S-EPMC5338227 | BioStudies | 2016-01-01

REPOSITORIES: biostudies

Similar Datasets

1000-01-01 | S-EPMC1301174 | BioStudies
2005-01-01 | S-EPMC1237137 | BioStudies
2019-01-01 | S-EPMC6706346 | BioStudies
1999-01-01 | S-EPMC17713 | BioStudies
2013-01-01 | S-EPMC3750062 | BioStudies
1000-01-01 | S-EPMC2191659 | BioStudies
2018-01-01 | S-EPMC6103880 | BioStudies
2011-01-01 | S-EPMC3509772 | BioStudies
1000-01-01 | S-EPMC3742182 | BioStudies
2013-01-01 | S-EPMC3585046 | BioStudies