Glutamine-181 is crucial in the enzymatic activity and substrate specificity of human endoplasmic-reticulum aminopeptidase-1

Biochemical Journal

Volumn 416, Issue 1, 2008, Pages 109-115

  Goto, Yoshikuni ^a   Tanji, Hiroe ^a   Hattori, Akira ^b   Tsujimoto, Masafumi ^a  

^a RIKEN   (Japan)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

Endoplasmic reticulum aminopeptidase 1 (ERAP 1); Oxytocinase subfamily; Placental leucine aminopeptidase; Site directed mutagenesis; Substrate specificity

Indexed keywords

ENDOPLASMIC-RETICULUM AMINOPEPTIDASE-1 (ERAP-1); OXYTOCINASE SUBFAMILY; PLACENTAL LEUCINE AMINOPEPTIDASE; SITE-DIRECTED MUTAGENESIS; SUBSTRATE SPECIFICITY;

AMINATION; AMINES; AMINO ACIDS; BLOOD PRESSURE; ENZYMES; MUTAGENESIS; ORGANIC ACIDS; PEPTIDES;

SUBSTRATES;

AMINOPEPTIDASE; ASPARTIC ACID; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1; GLUTAMINE; UNCLASSIFIED DRUG; AMASTATIN; ARTS 1 PROTEIN, HUMAN; ARTS-1 PROTEIN, HUMAN; PEPTIDE; ZINC;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; HUMAN; HUMAN CELL; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN CLEAVAGE; SITE DIRECTED MUTAGENESIS; AMINO ACID SEQUENCE; CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; ENZYME ACTIVE SITE; GENETICS; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY;

AMINO ACID SEQUENCE; AMINOPEPTIDASES; CATALYTIC DOMAIN; CELL LINE; GLUTAMINE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; SUBSTRATE SPECIFICITY; ZINC;

EID: 56049109055     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080965     Document Type: Article

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