Document Detail


A carbon-skeleton walk: a novel double rearrangement of glutaryl-CoA catalyzed by the human methylmalonyl-CoA mutase.
MedLine Citation:
PMID:  8722121     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
R Padmakumar; R Banerjee
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  BioFactors (Oxford, England)     Volume:  5     ISSN:  0951-6433     ISO Abbreviation:  Biofactors     Publication Date:    1995-1996
Date Detail:
Created Date:  1997-01-17     Completed Date:  1997-01-17     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8807441     Medline TA:  Biofactors     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  83-6     Citation Subset:  IM    
Affiliation:
Biochemistry Department, Beadle Center, University of Nebraska, Lincoln 68588-0664, USA.
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MeSH Terms
Descriptor/Qualifier:
Acyl Coenzyme A / chemistry*
Carbon / chemistry*
Catalysis
Humans
Methylmalonyl-CoA Mutase / chemistry*
Molecular Structure
Grant Support
ID/Acronym/Agency:
DK45776/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
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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