Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition

Protein Science

Volumn 11, Issue 9, 2002, Pages 2237-2246

  Ray, Kallol ^a   Hines, Christina S ^a   Rodgers, David W ^a  

^a UNIVERSITY OF KENTUCKY   (United States)

Author keywords

Model; Neurolysin; Specificity; Substrate; Thimet oligopeptidase

Indexed keywords

CYSTEINE; DISULFIDE; NEUROLYSIN; PHORATE; PROTEINASE; THIMET OLIGOPEPTIDASE; METALLOPROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME LOCALIZATION; ENZYME MODIFICATION; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; GENE MAPPING; MOLECULAR MODEL; MOLECULAR RECOGNITION; PRIORITY JOURNAL; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PEPTIDE MAPPING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; RAT; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE MAPPING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RATS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, PROTEIN; SUBSTRATE SPECIFICITY; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; ANIMALS;

EID: 0036708007     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0216302     Document Type: Article

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