Mutations at the S1 sites of methionine aminopeptidases from Escherichia coli and Homo sapiens reveal the residues critical for substrate specificity

Journal of Biological Chemistry

Volumn 279, Issue 20, 2004, Pages 21128-21134

  Li, Jing Ya ^a   Cui, Yong Mei ^a   Chen, Ling Ling ^a   Gu, Min ^a   Li, Jia ^a   Nan, Fa Jun ^a,c   Ye, Qi Zhuang ^a,b  

^a SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^b UNIVERSITY OF KANSAS   (United States)

^c Zhangjiang High tech Park   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; ESCHERICHIA COLI; HYDROPHOBICITY; POLYPEPTIDES; SYNTHESIS (CHEMICAL);

MUTATION; THIOPEPTOLIDES;

BIOCHEMISTRY;

ALANINE; AMINO ACID; CYSTEINE; GLYCINE; METHIONINE; METHIONYL AMINOPEPTIDASE; PHENYLALANINE; POLYPEPTIDE; TRYPTOPHAN;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIUM MUTANT; ENZYME ACTIVE SITE; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE MUTATION; HYDROLYSIS; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; RESIDUE ANALYSIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA; ESCHERICHIA COLI; HOMO; HOMO SAPIENS;

EID: 2442686862     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M401679200     Document Type: Article

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