English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8- ribityllumazine

Gerhardt, S., Schott, A. K., Kairies, N., Cushman, M., Illarionov, B., Eisenreich, W., et al. (2002). Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8- ribityllumazine. Structure, 10(10), 1371-1381.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Structure

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Gerhardt, S.1, Author              
Schott, A. K., Author
Kairies, N.1, Author              
Cushman, M., Author
Illarionov, B., Author
Eisenreich, W., Author
Bacher, A., Author
Huber, R.1, Author              
Steinbacher, S.1, Author              
Fischer, M., Author
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

Content

show
hide
Free keywords: biosynthesis of riboflavin; riboflavin synthase; X-ray structure; Schizosaccharomyces pombe; reaction mechanism
 Abstract: Riboflavin synthase catalyzes the disproportionation of 6,7- dimethyl-8-ribityllumazine affording riboflavin and 5-amino-6- ribitylamino-2,4(1H,3H)-pyrimidinedione. We have determined the structure of riboflavin synthase from Schizosaccharomyces pombe in complex with the substrate analog, 6-carboxyethyl-7-oxo-8- ribityllumazine at 2.1 Angstrom resolution. In contrast to the homotrimeric solution state of native riboflavin synthase, we found the enzyme to be monomeric in the crystal structure. Structural comparison of the riboflavin synthases of S. pombe and Escherichia coli suggests oligomer contact sites and delineates the catalytic site for dimerization of the substrate and subsequent fragmentation of the pentacyclic intermediate. The pentacyclic substrate dimer was modeled into the proposed active site, and its stereochemical features were determined. The model suggests that the substrate molecule at the C- terminal domain donates a four-carbon unit to the substrate molecule bound at the N-terminal domain of an adjacent subunit in the oligomer.

Details

show
hide
Language(s): eng - English
 Dates: 2002-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41754
ISI: 000178475400011
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Structure
  Alternative Title : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 10 (10) Sequence Number: - Start / End Page: 1371 - 1381 Identifier: ISSN: 0969-2126