1aw5
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5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE
OverviewOverview
5-Aminolaevulinate dehydratase (ALAD) is a homo-octameric metallo-enzyme, that catalyses the formation of porphobilinogen from 5-aminolaevulinic, acid. The structure of the yeast enzyme has been solved to 2.3 A, resolution, revealing that each subunit adopts a TIM barrel fold with a 39, residue N-terminal arm. Pairs of monomers wrap their arms around each, other to form compact dimers and these associate to form a 422 symmetric, octamer. All eight active sites are on the surface of the octamer and, possess two lysine residues (210 and 263), one of which, Lys 263, forms a, Schiff base link to the substrate. The two lysine side chains are close to, two zinc binding sites one of which is formed by three cysteine residues, (133, 135 and 143) while the other involves Cys 234 and His 142. ALAD has, features at its active site that are common to both metallo- and Schiff, base-aldolases and therefore represents an intriguing combination of both, classes of enzyme. Lead ions, which inhibit ALAD potently, replace the, zinc bound to the enzyme's unique triple-cysteine site.
About this StructureAbout this Structure
1AW5 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase., Erskine PT, Senior N, Awan S, Lambert R, Lewis G, Tickle IJ, Sarwar M, Spencer P, Thomas P, Warren MJ, Shoolingin-Jordan PM, Wood SP, Cooper JB, Nat Struct Biol. 1997 Dec;4(12):1025-31. PMID:9406553
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