Two non-redundant fragments in the N-terminal peptide of human cytosolic methionyl-tRNA synthetase were indispensable for the multi-synthetase complex incorporation and enzyme activity

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 2, 2009, Pages 347-354

  He, Ran ^a   Zu, Li Dong ^a   Yao, Peng ^a   Chen, Xin ^a   Wang, En Duo ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

Author keywords

Activity; Human cytoplasm; Incorporation; Methionyl tRNA synthetase; Multi synthetase complex

Indexed keywords

GLUTATHIONE TRANSFERASE; METHIONINE TRANSFER RNA LIGASE;

AMINO TERMINAL SEQUENCE; AMINOACYLATION; ARTICLE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; CYTOPLASM; ENZYME ACTIVITY; ENZYME MECHANISM; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CELL LINE; CYTOSOL; HUMANS; METHIONINE-TRNA LIGASE; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; PROLINE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

EID: 58149302677     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.11.003     Document Type: Article

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