2c0a: Difference between revisions
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Revision as of 17:48, 30 October 2007
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MECHANISM OF THE CLASS I KDPG ALDOLASE
OverviewOverview
In vivo, 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase catalyzes the, reversible, stereospecific retro-aldol cleavage of KDPG to pyruvate and, D-glyceraldehyde-3-phosphate. The enzyme is a lysine-dependent (Class I), aldolase that functions through the intermediacy of a Schiff base. Here, we propose a mechanism for this enzyme based on crystallographic studies, of wild-type and mutant aldolases. The three dimensional structure of KDPG, aldolase from the thermophile Thermotoga maritima was determined to 1.9A., The structure is the standard alpha/beta barrel observed for all Class I, aldolases. At the active site Lys we observe clear density for a pyruvate, Schiff base. Density for a sulfate ion bound in a conserved cluster of, residues close to the Schiff base is also observed. We have ... [(full description)]
About this StructureAbout this Structure
2C0A is a [Single protein] structure of sequence from [Escherichia coli] with PO4 as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Mechanism of the Class I KDPG aldolase., Fullerton SW, Griffiths JS, Merkel AB, Cheriyan M, Wymer NJ, Hutchins MJ, Fierke CA, Toone EJ, Naismith JH, Bioorg Med Chem. 2006 May 1;14(9):3002-10. Epub 2006 Jan 5. PMID:16403639
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