| A carbon-skeleton walk: a novel double rearrangement of glutaryl-CoA catalyzed by the human methylmalonyl-CoA mutase. | |
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MedLine Citation:
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PMID: 8722121 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Methylmalonyl-CoA mutase is a member of the coenzyme B12-dependent family of isomerases and interconverts methylmalonyl-CoA and succinyl-CoA. We have examined the ability of the enzyme to effect a double rearrangement reaction when presented with glutaryl-CoA, a substrate analog with a three-carbon template on which two successive 1,2 migrations can occur. Our results demonstrate that the enzyme converts glutaryl-CoA to both methylsuccinyl-CoA and ethylmalonyl-CoA. To our knowledge, this is the first example of a double rearrangement reaction catalyzed by a coenzyme B12-dependent enzyme. |
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Authors:
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R Padmakumar; R Banerjee |
Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: BioFactors (Oxford, England) Volume: 5 ISSN: 0951-6433 ISO Abbreviation: Biofactors Publication Date: 1995-1996 |
Date Detail:
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Created Date: 1997-01-17 Completed Date: 1997-01-17 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 8807441 Medline TA: Biofactors Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 83-6 Citation Subset: IM |
Affiliation:
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Biochemistry Department, Beadle Center, University of Nebraska, Lincoln 68588-0664, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acyl Coenzyme A
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chemistry* Carbon / chemistry* Catalysis Humans Methylmalonyl-CoA Mutase / chemistry* Molecular Structure |
| Grant Support | |
ID/Acronym/Agency:
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DK45776/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Acyl Coenzyme A; 0/ethylmalonyl-coenzyme A; 0/methylsuccinyl-coenzyme A; 3131-84-8/glutaryl-coenzyme A; 7440-44-0/Carbon; EC 5.4.99.2/Methylmalonyl-CoA Mutase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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