1ips
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Penicillin antibiotics are all produced from fermentation-derived, penicillins because their chemical synthesis is not commercially viable., The key step in penicillin biosynthesis, in which both the beta-lactam and, thiazolidine rings of the nucleus are created, is mediated by, isopenicillin N synthase (IPNS), which binds ferrous iron and uses, dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical, precedent, IPNS catalyses the transfer of four hydrogen atoms from its, tripeptide substrate to dioxygen forming, in a single reaction, the, complete bicyclic nucleus of the penicillins. We now report the structure, of IPNS complexed with manganese, which reveals the active site is, unusually buried within a 'jelly-roll' motif and lined by hydrophobic, residues, and suggest .. | + | Penicillin antibiotics are all produced from fermentation-derived, penicillins because their chemical synthesis is not commercially viable., The key step in penicillin biosynthesis, in which both the beta-lactam and, thiazolidine rings of the nucleus are created, is mediated by, isopenicillin N synthase (IPNS), which binds ferrous iron and uses, dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical, precedent, IPNS catalyses the transfer of four hydrogen atoms from its, tripeptide substrate to dioxygen forming, in a single reaction, the, complete bicyclic nucleus of the penicillins. We now report the structure, of IPNS complexed with manganese, which reveals the active site is, unusually buried within a 'jelly-roll' motif and lined by hydrophobic, residues, and suggest how this structure permits the process of penicillin, formation. Sequence analyses indicate IPNS, 1-aminocyclopropane-1-carboxylic acid oxidase and many of the, 2-oxo-acid-dependent oxygenases contain a conserved jelly-roll motif, forming a new structural family of enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1IPS is a | + | 1IPS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: SA and SB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IPS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:58:49 2007'' |
Revision as of 12:53, 5 November 2007
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ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)
Overview
Penicillin antibiotics are all produced from fermentation-derived, penicillins because their chemical synthesis is not commercially viable., The key step in penicillin biosynthesis, in which both the beta-lactam and, thiazolidine rings of the nucleus are created, is mediated by, isopenicillin N synthase (IPNS), which binds ferrous iron and uses, dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical, precedent, IPNS catalyses the transfer of four hydrogen atoms from its, tripeptide substrate to dioxygen forming, in a single reaction, the, complete bicyclic nucleus of the penicillins. We now report the structure, of IPNS complexed with manganese, which reveals the active site is, unusually buried within a 'jelly-roll' motif and lined by hydrophobic, residues, and suggest how this structure permits the process of penicillin, formation. Sequence analyses indicate IPNS, 1-aminocyclopropane-1-carboxylic acid oxidase and many of the, 2-oxo-acid-dependent oxygenases contain a conserved jelly-roll motif, forming a new structural family of enzymes.
About this Structure
1IPS is a Single protein structure of sequence from Emericella nidulans with MN as ligand. Structure known Active Sites: SA and SB. Full crystallographic information is available from OCA.
Reference
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes., Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE, Nature. 1995 Jun 22;375(6533):700-4. PMID:7791906
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