Structural insights into the catalytic mechanism of sphingomyelinases D and evolutionary relationship to glycerophosphodiester phosphodiesterases

Biochemical and Biophysical Research Communications

Volumn 342, Issue 1, 2006, Pages 323-329

  Murakami, Mário T ^a   Freitas Fernandes Pedrosa, Matheus ^b   De Andrade, Sonia A ^b   Gabdoulkhakov, Azat ^c   Betzel, Christian ^d   Tambourgi, Denise V ^b   Arni, Raghuvir K ^a,b  

^a SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

^b INSTITUTO BUTANTAN   (Brazil)

^c INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^d UNIVERSITY OF HAMBURG   (Germany)

Author keywords

Catalytic mechanism; Crystal structure; Glycerophosphodiester phosphodiesterases; Hydrodynamic behavior; Mg2+ binding site; Sphingomyelinase D

Indexed keywords

AMINO ACID; DISULFIDE; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE; MAGNESIUM ION; PHOSPHODIESTERASE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOMYELINASE D; SPIDER VENOM; SULFATE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STRUCTURE; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SPIDER; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CATIONS, DIVALENT; CRYSTALLOGRAPHY, X-RAY; EVOLUTION, MOLECULAR; HYDROGEN BONDING; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHORIC DIESTER HYDROLASES; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN;

ARANEAE; LOXOSCELES;

EID: 32644488753     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.01.123     Document Type: Article

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