Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Catalytic promiscuity in the alpha/beta-hydrolase superfamily: Hydroxamic acid formation, C-C bondformation, ester and thioester hydrolysis in the C-C hydrolase family

Tools
- Tools
+ Tools

Li, C. (Chen), Hassler, Melanie and Bugg, Tim (2008) Catalytic promiscuity in the alpha/beta-hydrolase superfamily: Hydroxamic acid formation, C-C bondformation, ester and thioester hydrolysis in the C-C hydrolase family. Chembiochem, Vol.9 (No.1). pp. 71-76. doi:10.1002/cbic.200700428 ISSN 1439-4227.

Research output not available from this repository.

Request-a-Copy directly from author or use local Library Get it For Me service.

Official URL: http://dx.doi.org/10.1002/cbic.200700428

Request Changes to record.

Abstract

The haloperoxidase family of alpha/beta-hydrolases contains enzymes of several different catalytic activities, including esterases, C-C hydrolases and cofactor-independent haloperoxidases (perhydrolases), but the molecular basis of this catalytic promiscuity is not fully understood. The C-C hydrolase enzyme MhpC from E. coli is shown to possess esterase and thioesterase activity, and the ability to activate hydroxylamine as a nucleophile to form hydroxamic acid products. The ratio of these activities was examined for nine site-directed mutant enzymes that contained mutations at nonessential residues in the enzyme active site. Higher levels of esterase and thioesterase activity were found in mutants Phe173Gly and Trp264Gly; this might be due to increased amounts of space in the active site. Higher levels of hydroxamic acid formation activity were found in mutant Asn109His-a mutation found in many haloperoxidase enzymes. Wild-type and mutant MhpC enzymes were also capable of C-C bond formation in organic solvents, and the highest activity was observed in nonpolar solvents. The results provide experimental support for the catalytic promiscuity shown in this family of enzymes, and indicate that differences in catalytic function can be introduced by point mutations.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Library of Congress Subject Headings (LCSH): Hydrolase, Hydrolysis, Esterases, Catalysis
Journal or Publication Title: Chembiochem
Publisher: Wiley - V C H Verlag GmbH & Co. KGaA
ISSN: 1439-4227
Official Date: 4 January 2008
Dates:
DateEvent
4 January 2008Published
Volume: Vol.9
Number: No.1
Number of Pages: 6
Page Range: pp. 71-76
DOI: 10.1002/cbic.200700428
Status: Peer Reviewed
Publication Status: Published

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us