Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease

Biochemical and Biophysical Research Communications

Volumn 391, Issue 1, 2010, Pages 431-436

  Kim, Doyoun ^a   San, Boi Hoa ^a,b   Moh, Sang Hyun ^a,b   Park, Hyejin ^a   Kim, Dong Young ^a   Lee, Sangho ^c   Kim, Kyeong Kyu ^a,b  

^a Sungkyunkwan University School of Medicine   (South Korea)

^b Sungkyunkwan University   (South Korea)

^c Sungkyunkwan University   (South Korea)

Author keywords

Glutamyl aminopeptidase; M42 family protease; PepA; Streptococcus pneumoniae; Substrate specificity; Tetrahedral aminopeptidase

Indexed keywords

ARGININE; BACTERIAL PROTEIN; PEPA PROTEIN; PROTEINASE; UNCLASSIFIED DRUG;

ACIDITY; AMINO TERMINAL SEQUENCE; ARTICLE; COMPARATIVE STUDY; CRYSTAL STRUCTURE; ELECTRICITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ALIGNMENT; STREPTOCOCCUS PNEUMONIAE;

AMINO ACID SEQUENCE; ARGININE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; GLUTAMYL AMINOPEPTIDASE; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; PROTEIN SUBUNITS; STATIC ELECTRICITY; STREPTOCOCCUS PNEUMONIAE; SUBSTRATE SPECIFICITY;

STREPTOCOCCUS PNEUMONIAE;

EID: 72949106693     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.11.075     Document Type: Article

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