EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity

BMC Microbiology

Volumn 8, Issue , 2008, Pages

  Allhorn, Maria ^a   Olsén, Arne ^a,b   Collin, Mattias ^a  

^a LUND UNIVERSITY   (Sweden)

^b ASTRAZENECA R AND D   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; IMMUNOGLOBULIN G; PROTEIN; PROTEIN ENDOS; PROTEIN SPEB; TRYPTOPHAN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CYSTEINE PROTEINASE; GLYCOSIDASE; POLYSACCHARIDE;

ARTICLE; BACTERIAL GROWTH; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME RELEASE; HYDROLYSIS; IN VITRO STUDY; MATURATION; NONHUMAN; STREPTOCOCCUS PYOGENES; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION; WESTERN BLOTTING;

BACTERIA (MICROORGANISMS); STREPTOCOCCUS PYOGENES;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BLOTTING, WESTERN; CYSTEINE ENDOPEPTIDASES; GLUTAMIC ACID; GLYCOSIDE HYDROLASES; HYDROLYSIS; IMMUNOGLOBULIN G; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POLYSACCHARIDES; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; STREPTOCOCCUS PYOGENES; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTOPHAN;

EID: 40849097885     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-8-3     Document Type: Article

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