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Phenylalanyl‐tRNA and Seryl‐tRNA from Synthetases Baker's Yeast
Author(s) -
FREIST Wolfgang,
HAAR Friedrich,
SPRINZL Mathias,
CRAMER Friedrich
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10313.x
Subject(s) - aminoacylation , transfer rna , mechanism (biology) , yeast , aminoacyl trna synthetase , substrate specificity , biochemistry , chemistry , biology , rna , enzyme , philosophy , gene , epistemology
Eighteen analogs of ATP have been tested in the aminoacylation reaction of phenylalanyl‐tRNA and seryl‐tRNA synthetases from baker's yeast. Four compounds. are substrates for phenylalanylLRNA syntiteiase, live for seryl‐tRNA synthetase, one compound is an inhibitor for both enzymes; their K m and K i and V values have been determined. The substrate specificity shows that for the catalytic action of both enzymes with these substrates positions 6, 7, 8 and 9 of the purine moiety and positions 2′ and 3′ of the ribose moiety are important.

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