Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalysed by the methionyl-tRNA synthetase from Escherichia coli

Journal of Molecular Biology

Volumn 217, Issue 3, 1991, Pages 465-475

  Mechulam, Yves ^a   Dardel, Frédéric ^a   Le Corre, Daniel ^a   Blanquet, Sylvain ^a   Fayat, Guy ^a  

^a LABORATOIRE DE BIOCHIMIE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; LYSINE; METHIONINE TRANSFER RNA LIGASE;

AMINO ACID SEQUENCE; ARTICLE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATE; AMINO ACID ACTIVATION; AMINO ACID SEQUENCE; BASE SEQUENCE; CLONING, MOLECULAR; DIPHOSPHATES; DNA MUTATIONAL ANALYSIS; ESCHERICHIA COLI; KINETICS; METHIONINE; METHIONINE-TRNA LIGASE; MOLECULAR SEQUENCE DATA; RNA, TRANSFER, MET; STRUCTURE-ACTIVITY RELATIONSHIP; SUPPORT, NON-U.S. GOV'T; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 0026059951     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/0022-2836(91)90750-Z     Document Type: Article

References (23)

1. Affinity labeling of Escherichia coli phenylalanyl-tRNA synthetase at the binding site for tRNAPhe
2. An Algorithm for Least-Squares Estimation of Nonlinear Parameters