2c13: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
Porphobilinogen synthase catalyzes the first committed step of the | 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. | ||
==About this Structure== | ==About this Structure== | ||
| Line 17: | Line 17: | ||
[[Category: Frere, F.]] | [[Category: Frere, F.]] | ||
[[Category: Gacond, S.]] | [[Category: Gacond, S.]] | ||
[[Category: Heinz, D | [[Category: Heinz, D W.]] | ||
[[Category: Neier, R.]] | [[Category: Neier, R.]] | ||
[[Category: Nentwich, M.]] | [[Category: Nentwich, M.]] | ||
| Line 32: | Line 32: | ||
[[Category: porphyrin biosynthesis]] | [[Category: porphyrin biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:45 2008'' | ||
Revision as of 17:43, 21 February 2008
|
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 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.
About this StructureAbout this Structure
2C13 is a Single protein structure of sequence from Pseudomonas aeruginosa with , , , and as ligands. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 16:43:45 2008