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1hb3
From Proteopedia
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[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
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Revision as of 13:29, 30 October 2007
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ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN EXPOSED PRODUCT FROM ANAEROBIC ACOV FE COMPLEX)
Overview
BACKGROUND: Isopenicillin N synthase (IPNS) catalyses formation of, bicyclic isopenicillin N, precursor to all penicillin and cephalosporin, antibiotics, from the linear tripeptide, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine. IPNS is a non-haem, iron(II)-dependent enzyme which utilises the full oxidising potential of, molecular oxygen in catalysing the bicyclisation reaction. The reaction, mechanism is believed to involve initial formation of the beta-lactam ring, (via a thioaldehyde intermediate) to give an iron(IV)-oxo species, which, then mediates closure of the 5-membered thiazolidine ring. RESULTS: Here, we report experiments employing time-resolved crystallography to observe, turnover of an isosteric substrate analogue designed to intercept the, catalytic pathway at an early ... [(full description)]
About this Structure
1HB3 is a [Single protein] structure of sequence from [Emericella nidulans] with SO4, FE2 and SCV as [ligands]. Structure known Active Site: SCV. Full crystallographic information is available from [OCA].
Reference
Alternative oxidation by isopenicillin N synthase observed by X-ray diffraction., Ogle JM, Clifton IJ, Rutledge PJ, Elkins JM, Burzlaff NI, Adlington RM, Roach PL, Baldwin JE, Chem Biol. 2001 Dec;8(12):1231-7. PMID:11755401
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