1zen
From Proteopedia
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[[Image:1zen.gif|left|200px]] | [[Image:1zen.gif|left|200px]] | ||
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| - | | | + | {{STRUCTURE_1zen| PDB=1zen | SCENE= }} |
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'''CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE''' | '''CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE''' | ||
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[[Category: Hunter, W N.]] | [[Category: Hunter, W N.]] | ||
[[Category: Leonard, G A.]] | [[Category: Leonard, G A.]] | ||
| - | [[Category: | + | [[Category: Aldehyde]] |
| - | [[Category: | + | [[Category: Glycolysis]] |
| - | [[Category: | + | [[Category: Lyase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:31:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:31, 3 May 2008
CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE
Overview
BACLGROUND: 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 A 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 A 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.
About this Structure
1ZEN is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1ZEN with [The Glycolytic Enzymes]. Full crystallographic information is available from OCA.
Reference
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., Cooper SJ, Leonard GA, McSweeney SM, Thompson AW, Naismith JH, Qamar S, Plater A, Berry A, Hunter WN, Structure. 1996 Nov 15;4(11):1303-15. PMID:8939754 Page seeded by OCA on Sat May 3 17:31:57 2008
