1w8s
From Proteopedia
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THE MECHANISM OF THE SCHIFF BASE FORMING FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE: STRUCTURAL ANALYSIS OF REACTION INTERMEDIATES
Overview
The glycolytic enzyme fructose-1,6-bisphosphate aldolase (FBPA) catalyzes, the reversible cleavage of fructose 1,6-bisphosphate to glyceraldehyde, 3-phosphate and dihydroxyacetone phosphate. Catalysis of Schiff base, forming class I FBPA relies on a number of intermediates covalently bound, to the catalytic lysine. Using active site mutants of FBPA I from, Thermoproteus tenax, we have solved the crystal structures of the enzyme, covalently bound to the carbinolamine of the substrate fructose, 1,6-bisphosphate and noncovalently bound to the cyclic form of the, substrate. The structures, determined at a resolution of 1.9 A and refined, to crystallographic R factors of 0.148 and 0.149, respectively, represent, the first view of any FBPA I in these two stages of the reaction pathway, and ... [(full description)]
About this Structure
1W8S is a [Single protein] structure of sequence from [Thermoproteus tenax] with FBP as [ligand]. Active as [Fructose-bisphosphate aldolase], with EC number [4.1.2.13]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates., Lorentzen E, Siebers B, Hensel R, Pohl E, Biochemistry. 2005 Mar 22;44(11):4222-9. PMID:15766250
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