Examination of a reaction intermediate in the active site of riboflavin synthase

Ya-Jun Zheng; Douglas B Jordan; Der-Ing Liao

doi:10.1016/s0045-2068(03)00029-4

Examination of a reaction intermediate in the active site of riboflavin synthase

Bioorg Chem. 2003 Aug;31(4):278-87. doi: 10.1016/s0045-2068(03)00029-4.

Authors

Ya-Jun Zheng¹, Douglas B Jordan, Der-Ing Liao

Affiliation

¹ DuPont Agricultural Products, Stine-Haskell Research Center, 1094 Elkton Road, Post Office Box 30, Newark, DE 19714, USA. ya-jun.zheng@usa.dupont.com

PMID: 12877878
DOI: 10.1016/s0045-2068(03)00029-4

Abstract

The riboflavin synthase catalyzed reaction proceeds through a pentacyclic intermediate of undetermined stereochemistry. Calculations at the B3LYP/6-31G(d) level of theory indicate that the trans pentacyclic structure is favored over the cis by 3.3kcal/mol. A model of the the trans, but not the cis, pentacycle in the enzyme active site shows good fitness and the availability of highly conserved protein residues for catalytic interactions. The model of the trans intermediate complements the model of the two substrates in the active site and allows for a hypothetical mechanism of the roles of specific protein residues in catalysis to be proposed.

MeSH terms

Binding Sites
Catalysis
Models, Chemical
Models, Molecular
Molecular Structure
Riboflavin Synthase / chemistry*
Riboflavin Synthase / metabolism*
Stereoisomerism

Substances

Riboflavin Synthase