Affordable Access

Publisher Website

The porphobilinogen synthase catalyzed reaction mechanism

Authors
Journal
Bioorganic Chemistry
0045-2068
Publisher
Elsevier
Publication Date
Volume
32
Issue
5
Identifiers
DOI: 10.1016/j.bioorg.2004.05.010
Keywords
  • Porphobilinogen Synthase
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract Porphobilinogen synthase (PBGS) catalyzes the first common reaction in the biosynthesis of the tetrapyrroles, the asymmetric condensation of two molecules of δ-aminolevulinic acid to form porphobilinogen. There is a variable requirement for an essential active site zinc that necessitates consideration of PBGS as an enzyme that may exhibit phylogenetic diversity in its chemical reaction mechanism. Recent crystal structures suggest reaction mechanisms that involve two covalent Schiff base linkages between adjacent active site lysine residues and each of the two substrate molecules. The reaction appears to stall at a covalently bound almost-product intermediate that is poised for breakdown to product upon binding of a substrate molecule to an adjacent active site and a subsequent conformational change.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

The porphobilinogen synthase catalyzed reaction me...

on Bioorganic chemistry October 2004

Dissection of the early steps in the porphobilinog...

on Journal of Biological Chemistr... Jul 15, 1986

Probing the mechanism of 1,4-conjugate elimination...

on Journal of the American Chemic... Dec 26, 2012
More articles like this..