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Catalysis of peptide bond formation by histidyl-histidine in a fluctuating clay environmentThe condensation of glycine to form oligoglycines during wet-dry fluctuations on clay surfaces was enhanced up to threefold or greater by small amounts of histidyl-histidine. In addition, higher relative yields of the longer oligomers were produced. Other specific dipeptides tested gave no enhancement, and imidazole, histidine, and N-acetylhistidine gave only slight enhancements. Histidyl-histidine apparently acts as a true catalyst (in the sense of repeatedly catalyzing the reaction), since up to 52 nmol of additional glycine were incorporated into oligoglycine for each nmol of catalyst added. This is the first known instance of a peptide or similar molecule demonstrating a catalytic turnover number greater than unity in a prebiotic oligomer synthesis reaction, and suggests that histidyl-histidine is a model for a primitive prebiotic proto-enzyme. Catalysis of peptide bond synthesis by a molecule which is itself a peptide implies that related systems may be capable of exhibiting autocatalytic growth.
Document ID
19810033521
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
White, D. H.
(Santa Clara Univ. CA, United States)
Erickson, J. C.
(Santa Clara, University Santa Clara, Calif., United States)
Date Acquired
August 11, 2013
Publication Date
December 1, 1980
Publication Information
Publication: Journal of Molecular Evolution
Volume: 16
Subject Category
Chemistry And Materials (General)
Accession Number
81A17925
Funding Number(s)
CONTRACT_GRANT: NCA2-OR-685-806
CONTRACT_GRANT: NCA2-OR-685-708
Distribution Limits
Public
Copyright
Other

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