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Structural studies on the reaction of isopenicillin N synthase with the truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine.

Abstract:

Isopenicillin N synthase (IPNS), a non-heme iron(II)-dependent oxidase, catalyzes conversion of the tripeptide delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-valine (ACV) to bicyclic isopenicillin N (IPN), concomitant with the reduction of dioxygen to two molecules of water. Incubation of the "truncated"substrate analogues delta-(l-alpha-aminoadipoyl)-l-cysteinyl-glycine (ACG) and delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alanine (ACA) with IPNS has previously been shown to afford acyclic produc...

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Publication status:
Published

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Publisher copy:
10.1021/bi047478q

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Journal:
Biochemistry
Volume:
44
Issue:
17
Pages:
6619-6628
Publication date:
2005-05-01
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Source identifiers:
33073
Language:
English
Keywords:
Pubs id:
pubs:33073
UUID:
uuid:04940aa2-5fd1-47b3-a1e7-d0dcf159ea2b
Local pid:
pubs:33073
Deposit date:
2012-12-19

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