| From mineral support to enzymatic catalysis--further assumptions for the evolutionary history of glyoxalase system. | |
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MedLine Citation:
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PMID: 9689946 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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M P Kalapos |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of theoretical biology Volume: 193 ISSN: 0022-5193 ISO Abbreviation: J. Theor. Biol. Publication Date: 1998 Jul |
Date Detail:
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Created Date: 1998-09-04 Completed Date: 1998-09-04 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0376342 Medline TA: J Theor Biol Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 91-8 Citation Subset: IM; S |
Affiliation:
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Theoretical Biology Research Group, Budapest, Hungary. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Catalysis Evolution, Chemical* Imidazoles / metabolism Lactoylglutathione Lyase / metabolism* Metals Sulfhydryl Compounds / metabolism |
| Chemical | |
Reg. No./Substance:
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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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