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| [[Image:1vgq.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1vgq| PDB=1vgq | SCENE= }} | | {{STRUCTURE_1vgq| PDB=1vgq | SCENE= }} |
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| '''Formyl-CoA transferase mutant Asp169 to Ala'''
| | ===Formyl-CoA transferase mutant Asp169 to Ala=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15213226}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15213226 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15213226}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Oxalate]] | | [[Category: Oxalate]] |
| [[Category: Oxalate degradation]] | | [[Category: Oxalate degradation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:31:19 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:52:49 2008'' |
