Identification and biochemical characterization of an acid sphingomyelinase-like protein from the bacterial plant pathogen Ralstonia solanacearum that hydrolyzes ATP to AMP but not sphingomyelin to ceramide

PLoS ONE

Volumn 9, Issue 8, 2014, Pages

  Airola, Michael V ^a   Tumolo, Jessica M ^b   Snider, Justin ^a   Hannun, Yusuf A ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACID SPHINGOMYELINASE LIKE PROTEIN; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; CERAMIDE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL PLANT DISEASE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SPECIFICITY; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PATHOGENICITY; PROTEIN EXPRESSION; PROTEIN FOLDING; RALSTONIA SOLANACEARUM; SEQUENCE HOMOLOGY; CHEMISTRY; ENZYMOLOGY; HUMAN; METABOLISM;

ADENOSINE MONOPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; HUMANS; HYDROLYSIS; RALSTONIA SOLANACEARUM; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOMYELINS; SUBSTRATE SPECIFICITY;

EID: 84923153267     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0105830     Document Type: Article

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