2j27

From Proteopedia

Revision as of 06:25, 30 October 2007

THE FUNCTIONAL ROLE OF THE CONSERVED ACTIVE SITE PROLINE OF TRIOSEPHOSPHATE ISOMERASE

Overview

The importance of the fully conserved active site proline, Pro168, for the, reaction mechanism of triosephosphate isomerase (TIM) has been, investigated by studying the enzymatic and crystallographic properties of, the P168A variant of trypanosomal TIM. In TIM, Pro168 follows the key, catalytic residue Glu167, situated at the beginning of the flexible active, site loop (loop 6). Turnover numbers of the P168A variant for its, substrates are reduced approximately 50-fold, whereas the Km values are, approximately 2 times lower. The affinity of the P168A variant for the, transition state analogue 2-phosphoglycolate (2PG) is reduced 5-fold. The, crystal structures of unliganded and liganded (2PG) P168A show that the, phosphate moiety of 2PG is bound similarly as in wild-type TIM, whereas, the ... [(full description)]

About this Structure

2J27 is a [Single protein] structure of sequence from [Trypanosoma brucei brucei] with PGA and SO4 as [ligands]. Active as [Isomerase], with EC number [5.3.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase(,)., Casteleijn MG, Alahuhta M, Groebel K, El-Sayed I, Augustyns K, Lambeir AM, Neubauer P, Wierenga RK, Biochemistry. 2006 Dec 26;45(51):15483-15494. Epub 2006 Dec 19. PMID:17176070

Page seeded by OCA on Tue Oct 30 08:30:36 2007