2c13: Difference between revisions
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[[Category: porphyrin biosynthesis]] | [[Category: porphyrin biosynthesis]] | ||
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Revision as of 17:49, 30 October 2007
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5-HYDROXY-LEVULINIC ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA
OverviewOverview
Porphobilinogen synthase catalyzes the first committed step of the, tetrapyrrole biosynthesis pathway. In an aldol-like condensation, two, molecules of 5-aminolevulinic acid (ALA) form the first pyrrole, porphobilinogen. Newly synthesized analogues of a reaction intermediate of, porphobilinogen synthase have been employed in studying the active site, and the catalytic mechanism of this early enzyme of tetrapyrrole, biosynthesis. This study combines structural and kinetic evaluation of the, inhibition potency of these inhibitors. In addition, one of the determined, protein structures provides for the first time structural evidence of a, magnesium ion in the active site. From these results, we can corroborate, an earlier postulated enzymatic mechanism that starts with formation of a, C-C ... [(full description)]
About this StructureAbout this Structure
2C13 is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with MG, CL, K, PGE and PEG as [ligands]. Active as [Porphobilinogen synthase], with EC number [4.2.1.24]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors., Frere F, Nentwich M, Gacond S, Heinz DW, Neier R, Frankenberg-Dinkel N, Biochemistry. 2006 Jul 11;45(27):8243-53. PMID:16819823
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