2j27
From Proteopedia
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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 [Triose-phosphate 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 17:22:34 2007
Categories: Single protein | Triose-phosphate isomerase | Trypanosoma brucei brucei | Alahuhta, M. | Augustyns, K. | Casteleijn, M.G. | El-Sayed, I. | Groebel, K. | Lambeir, A.M. | Neubauer, P. | Wierenga, R.K. | PGA | SO4 | 2-phospho glycolate | 2pg | Atomic resolution | Fatty acid biosynthesis | Gluconeogenesis | Glycolysis | Glycosome | Isomerase | Lipid synthesis | Loop7 | Pentose shunt | Point mutation | Protein engineering | Tim | Tim-barrel