Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes
Articolo
Data di Pubblicazione:
2004
Citazione:
Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes / S. Jonsson, S. Ricagno, Y. Lindqvist, N.G..J. Richards. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 279:34(2004 Aug), pp. 36003-36012.
Abstract:
Oxalobacter formigenes is an obligate anaerobe that colonizes the human gastrointestinal tract and employs oxalate breakdown to generate ATP in a novel process involving the interplay of two coupled enzymes and a membrane-bound oxalate:formate antiporter. Formyl-CoA transferase is a critical enzyme in oxalate-dependent ATP synthesis and is the first Class III CoA-transferase for which a high resolution, three-dimensional structure has been determined (Ricagno, S., Jonsson, S., Richards, N., and Lindqvist, Y. (2003) EMBO J. 22, 3210-3219). We now report the first detailed kinetic characterizations of recombinant, wild type formyl-CoA transferase and a number of site-specific mutants, which suggest that catalysis proceeds via a series of anhydride intermediates. Further evidence for this mechanistic proposal is provided by the x-ray crystallographic observation of an acylenzyme intermediate that is formed when formyl-CoA transferase is incubated with oxalyl-CoA. The catalytic mechanism of formyl-CoA transferase is therefore established and is almost certainly employed by all other members of the Class III CoA-transferase family.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
bacterial proteins; catalytic domain; coenzyme a-transferases; humans; kinetics; molecular structure; mutation; oxalobacter formigenes; protein conformation; recombinant proteins; structure-activity relationship; biochemistry; medicine (all); molecular biology; cell biology
Elenco autori:
S. Jonsson, S. Ricagno, Y. Lindqvist, N.G..J. Richards
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