USE OF BINDING-ENERGY IN CATALYSIS ANALYZED BY MUTAGENESIS OF THE TYROSYL-TRANSFER RNA-SYNTHETASE

[11] TRANSITION-STATE STABILIZATION IN THE MECHANISM OF TYROSYL-TRANSFER RNA-SYNTHETASE REVEALED BY PROTEIN ENGINEERING [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1985, 82 (23) : 7840 - 7844

[12] PROBING HISTIDINE SUBSTRATE INTERACTIONS IN TYROSYL-TRANSFER RNA-SYNTHETASE USING ASPARAGINE AND GLUTAMINE REPLACEMENTS [J]. BIOCHEMISTRY, 1985, 24 (19) : 5106 - 5109

[13] INTERACTION OF CRYSTALLINE TYROSYL-TRANSFER RNA-SYNTHETASE WITH ADENOSINE, ADENOSINE-MONOPHOSPHATE, ADENOSINE-TRIPHOSPHATE AND PYROPHOSPHATE IN THE PRESENCE OF TYROSINOL [J]. JOURNAL OF MOLECULAR BIOLOGY, 1984, 173 (04) : 477 - 485

[14] EDITING MECHANISMS IN AMINOACYLATION OF TRANSFER-RNA - ATP CONSUMPTION AND BINDING OF AMINOACYL-TRANSFER-RNA BY ELONGATION-FACTOR TU [J]. BIOCHEMISTRY, 1977, 16 (21) : 4731 - 4737

[15] Pauling L., 1946, CHEM ENG NEWS, V24, p[1375, 1375], DOI [10.1021/cen-v024n010, DOI 10.1021/CEN-V024N010.P1375]

[16] DELETION MUTAGENESIS USING AN M13 SPLINT - THE N-TERMINAL STRUCTURAL DOMAIN OF TYROSYL-TRANSFER RNA-SYNTHETASE (B-STEAROTHERMOPHILUS) CATALYZES THE FORMATION OF TYROSYL ADENYLATE [J]. EMBO JOURNAL, 1983, 2 (10) : 1827 - 1829

[17] HYDROGEN-BONDING IN ENZYMATIC CATALYSIS ANALYZED BY PROTEIN ENGINEERING [J]. NATURE, 1985, 316 (6029) : 656 - 657

[18] SITE-DIRECTED MUTAGENESIS AS A PROBE OF ENZYME STRUCTURE AND CATALYSIS - TYROSYL-TRANSFER RNA-SYNTHETASE CYSTEINE-35 TO GLYCINE-35 MUTATION [J]. BIOCHEMISTRY, 1983, 22 (15) : 3581 - 3586

[19] REDESIGNING ENZYME STRUCTURE BY SITE-DIRECTED MUTAGENESIS - TYROSYL TRANSFER-RNA SYNTHETASE AND ATP BINDING [J]. NATURE, 1982, 299 (5885) : 756 - 758

[11] TRANSITION-STATE STABILIZATION IN THE MECHANISM OF TYROSYL-TRANSFER RNA-SYNTHETASE REVEALED BY PROTEIN ENGINEERING [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1985, 82 (23) : 7840 - 7844

[12] PROBING HISTIDINE SUBSTRATE INTERACTIONS IN TYROSYL-TRANSFER RNA-SYNTHETASE USING ASPARAGINE AND GLUTAMINE REPLACEMENTS [J]. BIOCHEMISTRY, 1985, 24 (19) : 5106 - 5109

[13] INTERACTION OF CRYSTALLINE TYROSYL-TRANSFER RNA-SYNTHETASE WITH ADENOSINE, ADENOSINE-MONOPHOSPHATE, ADENOSINE-TRIPHOSPHATE AND PYROPHOSPHATE IN THE PRESENCE OF TYROSINOL [J]. JOURNAL OF MOLECULAR BIOLOGY, 1984, 173 (04) : 477 - 485

[14] EDITING MECHANISMS IN AMINOACYLATION OF TRANSFER-RNA - ATP CONSUMPTION AND BINDING OF AMINOACYL-TRANSFER-RNA BY ELONGATION-FACTOR TU [J]. BIOCHEMISTRY, 1977, 16 (21) : 4731 - 4737

[15] Pauling L., 1946, CHEM ENG NEWS, V24, p[1375, 1375], DOI [10.1021/cen-v024n010, DOI 10.1021/CEN-V024N010.P1375]

[16] DELETION MUTAGENESIS USING AN M13 SPLINT - THE N-TERMINAL STRUCTURAL DOMAIN OF TYROSYL-TRANSFER RNA-SYNTHETASE (B-STEAROTHERMOPHILUS) CATALYZES THE FORMATION OF TYROSYL ADENYLATE [J]. EMBO JOURNAL, 1983, 2 (10) : 1827 - 1829

[17] HYDROGEN-BONDING IN ENZYMATIC CATALYSIS ANALYZED BY PROTEIN ENGINEERING [J]. NATURE, 1985, 316 (6029) : 656 - 657

[18] SITE-DIRECTED MUTAGENESIS AS A PROBE OF ENZYME STRUCTURE AND CATALYSIS - TYROSYL-TRANSFER RNA-SYNTHETASE CYSTEINE-35 TO GLYCINE-35 MUTATION [J]. BIOCHEMISTRY, 1983, 22 (15) : 3581 - 3586

[19] REDESIGNING ENZYME STRUCTURE BY SITE-DIRECTED MUTAGENESIS - TYROSYL TRANSFER-RNA SYNTHETASE AND ATP BINDING [J]. NATURE, 1982, 299 (5885) : 756 - 758