Document Detail


From mineral support to enzymatic catalysis--further assumptions for the evolutionary history of glyoxalase system.
MedLine Citation:
PMID:  9689946     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In a previous paper we suggested that the methylglyoxalase pathway might have been an anaplerotic route for the archaic reductive citric acid cycle of surface metabolists at the early stage of evolution. The present paper tries to outline a possible way for the further development of enzyme catalysed glyoxalase path by separating the global process into several plausible evolutionary stages. A sequence of events is proposed which might have led to the emergence of energy rich bonds, especially to the formation of the thiol-ester bond. An explanation is given for the cofactor function of transition metals, as well. A proposition is also made for how nature may preserve molecular mechanisms using them for different purposes if the innovation has proved successful.
Authors:
M P Kalapos
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of theoretical biology     Volume:  193     ISSN:  0022-5193     ISO Abbreviation:  J. Theor. Biol.     Publication Date:  1998 Jul 
Date Detail:
Created Date:  1998-09-04     Completed Date:  1998-09-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376342     Medline TA:  J Theor Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  91-8     Citation Subset:  IM; S    
Affiliation:
Theoretical Biology Research Group, Budapest, Hungary.
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MeSH Terms
Descriptor/Qualifier:
Animals
Catalysis
Evolution, Chemical*
Imidazoles / metabolism
Lactoylglutathione Lyase / metabolism*
Metals
Sulfhydryl Compounds / metabolism
Chemical
Reg. No./Substance:
0/Imidazoles; 0/Metals; 0/Sulfhydryl Compounds; EC 4.4.1.5/Lactoylglutathione Lyase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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