His151 and His296 are the acid-base catalytic residues of Bacillus cereus sphingomyelinase in sphingomyelin hydrolysis

Biological and Pharmaceutical Bulletin

Volumn 26, Issue 7, 2003, Pages 920-926

  Obama, Takashi ^a   Fujii, Shinobu ^b   Ikezawa, Hiroh ^a   Ikeda, Kiyoshi ^b   Imagawa, Masayoshi ^a   Tsukamoto, Kikuo ^a  

^a NAGOYA CITY UNIVERSITY   (Japan)

^b OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

Active site; General acid base catalysis; Hemolysin; Phosphodiesterase; Phospholipase C

Indexed keywords

CERAMIDE; HEMOLYSIN; MAGNESIUM ION; PHOSPHORYLCHOLINE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; HISTIDINE;

ACID BASE BALANCE; ARTICLE; BACILLUS CEREUS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME MECHANISM; ENZYME STRUCTURE; GENE MUTATION; HEMOLYSIS; HYDROLYSIS; IONIZATION; MOLECULAR MODEL; NONHUMAN; PH MEASUREMENT; PROTEIN HYDROLYSIS; SITE DIRECTED MUTAGENESIS; THREE DIMENSIONAL IMAGING; CATALYSIS; COMPARATIVE STUDY; ENZYMOLOGY; GENETICS; METABOLISM; POINT MUTATION;

BACILLUS CEREUS; CATALYSIS; HISTIDINE; HYDROLYSIS; POINT MUTATION; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOMYELINS;

EID: 0842322518     PISSN: 09186158     EISSN: 13475215     Source Type: Journal    
DOI: 10.1248/bpb.26.920     Document Type: Article

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