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| The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold |
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| Author(s): Cooper SJ, Leonard GA, McSweeney SM, Thompson AW, Naismith JH, Qamar S, Plater A, Berry A, Hunter WN |
| Source: STRUCTURE Volume: 4 Issue: 11 Pages: 1303-1315 Published: NOV 15 1996 |
| Times Cited: 63 References: 55 |
| Abstract: Background: Aldolases catalyze a variety of condensation and cleavage reactions, with exquisite control on the stereochemistry. These enzymes, therefore, are attractive catalysts for synthetic chemistry. There are two classes of aldolase: class I aldolases utilize Schiff base formation with an active-site lysine whilst class II enzymes require a divalent metal ion, in particular zinc. Fructose-1,6-bisphosphate aldolase (FBP-aldolase) is used in gluconeogenesis and glycolysis; the enzyme controls the condensation of dihydroxyacetone phosphate with glyceraldehyde-3-phosphate to yield fructose-1,6-bisphosphate, Structures are available for class I FBP-aldolases but there is a paucity of detail on the class II enzymes. Characterization is sought to enable a dissection of structure/activity relationships which may assist the construction of designed aldolases for use as biocatalysts in synthetic chemistry. Results: The structure of the dimeric class II FBP-aldolase from Escherichia coli has been determined using data to 2.5 Angstrom resolution. The asymmetric unit is one subunit which presents a familiar fold, the (alpha/beta)(8) barrel. The active centre, at the C-terminal end of the barrel, contains a novel bimetallic-binding site with two metal ions 6.2 Angstrom apart. One ion, the identity of which is not certain, is buried and may play a structural or activating role. The other metal ion is zinc and is positioned at the surface of the barrel to participate in catalysis.
Conclusions: Comparison of the structure with a class II fuculose aldolase suggests that these enzymes may share a common mechanism. Nevertheless, the class II enzymes should be subdivided into two categories on consideration of subunit size and fold, quaternary structure and metal-ion binding sites. (C) Current Biology Ltd
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| Document Type: Article |
| Language: English |
Addresses:
1. UNIV MANCHESTER, DEPT CHEM, MANCHESTER M13 9PL, LANCS ENGLAND
2. EMBL, F-38043 GRENOBLE, FRANCE
3. UNIV LEEDS, DEPT BIOCHEM & MOL BIOL, LEEDS LS2 9JT, W YORKSHIRE ENGLAND |
| Publisher: CURRENT BIOLOGY LTD, 34-42 CLEVELAND STREET, LONDON, ENGLAND W1P 6LB |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: VT991 |
| ISSN: 0969-2126 |
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