Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
| العنوان: | Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes |
|---|---|
| المؤلفون: | Jack E. Baldwin, Karl Harlos, Inger Andersson, Ian J. Clifton, Geoffrey J. Barton, Peter L. Roach, Christopher J. Schofield, Janos Hajdu, Vilmos Fülöp |
| المصدر: | Scopus-Elsevier |
| بيانات النشر: | Springer Science and Business Media LLC, 1995. |
| سنة النشر: | 1995 |
| مصطلحات موضوعية: | Protein Conformation, Stereochemistry, Molecular Sequence Data, Thiazolidine, Isopenicillin N synthase, Tripeptide, Crystallography, X-Ray, Aspergillus nidulans, Catalysis, chemistry.chemical_compound, Protein structure, Computer Graphics, polycyclic compounds, Amino Acid Sequence, Cloning, Molecular, Antibacterial agent, Manganese, Binding Sites, Multidisciplinary, Sequence Homology, Amino Acid, biology, Deacetoxycephalosporin-C synthase, Bicyclic molecule, Active site, Recombinant Proteins, Acremonium, chemistry, biology.protein, Oxidoreductases |
| الوصف: | 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. |
| تدمد: | 1476-4687 0028-0836 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3abc50f73d6184a180e86eb5296a2c5 https://doi.org/10.1038/375700a0 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....f3abc50f73d6184a180e86eb5296a2c5 |
| قاعدة البيانات: | OpenAIRE |
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