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| [[Image:2c18.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2c18| PDB=2c18 | SCENE= }} | | {{STRUCTURE_2c18| PDB=2c18 | SCENE= }} |
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| '''5-(4-CARBOXY-2-OXO-BUTANE-1-SULFONYL)-4-OXO-PENTANOIC ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA'''
| | ===5-(4-CARBOXY-2-OXO-BUTANE-1-SULFONYL)-4-OXO-PENTANOIC ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA=== |
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| ==Overview==
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| 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 bond, linking C3 of the A-side ALA to C4 of the P-side ALA through an aldole addition. The obtained data are discussed with respect to the current literature.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16819823}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16819823 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16819823}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Porphobilinogen synthase]] | | [[Category: Porphobilinogen synthase]] |
| [[Category: Porphyrin biosynthesis]] | | [[Category: Porphyrin biosynthesis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:05:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:17:46 2008'' |