1ips: Difference between revisions
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'''ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)''' | '''ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)''' | ||
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[[Category: Roach, P L.]] | [[Category: Roach, P L.]] | ||
[[Category: Schofield, C J.]] | [[Category: Schofield, C J.]] | ||
[[Category: | [[Category: Antibiotic biosynthesis]] | ||
[[Category: | [[Category: B-lactam antibiotic]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Oxygenase]] | ||
[[Category: | [[Category: Penicillin biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:15:54 2008'' | |||
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Revision as of 17:15, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 20:15:54 2008
