Browse views: by Year, by Function, by GLF, by Subfunction, by Conference, by Journal

Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase.

Groff, Dan and Thielges, Megan C and Cellitti, Susan and Schultz, Peter and Romesberg, Floyd E (2009) Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase. Angewandte Chemie (International ed. in English), 48 (19). pp. 3478-3481. ISSN 1521-3773

Abstract

State secrets: Site-specific deuteration and FTIR studies reveal that Tyr100 in dihydrofolate reductase plays an important role in catalysis, with a strong electrostatic coupling occurring between Tyr100 and the charge that develops in the hydride-transfer transition state (see picture, NADP(+) purple, Tyr100 green). However, relaying correlated motions that facilitate catalysis from distal sites of the protein to the hydride donor may also be involved.

Item Type: Article
Related URLs:
Additional Information: archiving not allowed on institutional repository
Keywords: deuterium; dihydrofolate reductase; nzyme catalysis; IR spectroscopy; noncovalent interactions
Related URLs:
Date Deposited: 14 Dec 2009 13:49
Last Modified: 31 Jan 2013 00:57
URI: https://oak.novartis.com/id/eprint/1207

Search

Email Alerts

Register with OAK to receive email alerts for saved searches.