It was shown that a dipeptide, alanylhistidine, can act as a catalyst for the peptidyl transfer reaction in the absence of ribosomes between the amino acid moieties of phenylalanyl, lysyl, prolyl, and glycyl tRNAs depending on their model templates, poly U, poly A, poly C, and poly G, respectively. A template effect was observed: The peptidyl transfer reaction between tRNAGly molecules (anticodon GCC) occurred in the presence of poly G but not in the presence of poly C. The reaction was most efficient for the best stacked poly A (tRNALys) and least efficient for the worst stacked poly U (tRNAPhe).
Detection of the peptidyltransferase activity of a dipeptide, alanylhistidine, in the absence of ribosomes. Publishing Authors By Initials
Detection of the peptidyltransferase activity of a dipeptide, alanylhistidine, in the absence of ribosomes. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Journal of biochemistry
VOLUME: 119
Page Numbers: 832-4
Journal Abbreviation: J. Biochem.
ISSN: 0021-924X
DAY: 19
MONTH: May
YEAR: 1996
Detection of the peptidyltransferase activity of a dipeptide, alanylhistidine, in the absence of ribosomes. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 376600
Detection of the peptidyltransferase activity of a dipeptide, alanylhistidine, in the absence of ribosomes. Keywords Mesh Terms:
KEYWORDS: Templates, Genetic
MESH TERMS: metabolism
Chemical & Substance for Abstract: Detection of the peptidyltransferase activity of a dipeptide, alanylhistidine, in the absence of ribosomes. Information
Substance Name: Peptidyl Transferases
Registry Number: EC 2.3.2.12
Grant and Affiliation Information for Detection of the peptidyltransferase activity of a dipeptide, alanylhistidine, in the absence of ribosomes.
AFFILIATION: Institute of Space and Astronautical Science, Kanagawa.
Country: JAPAN
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MEDLINETA: J Biochem
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