Structural basis for nucleotide hydrolysis by the acid sphingomyelinase-like phosphodiesterase SMPDL3A

Journal of Biological Chemistry

Volumn 291, Issue 12, 2016, Pages 6376-6385

  Gorelik, Alexei ^a   Illes, Katalin ^a   Superti Furga, Giulio ^b   Nagar, Bhushan ^a  

^a MCGILL UNIVERSITY   (Canada)

^b ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CRYSTALS; ENZYMES; ESTERS; MOLECULES; NUCLEOTIDES; PHOSPHOLIPIDS;

ACID SPHINGOMYELINASE; COCRYSTAL STRUCTURE; HISTIDINE RESIDUES; NUCLEOSIDE DIPHOSPHATES; NUCLEOTIDE HYDROLYSIS; PHOSPHODIESTERASES; SUBSTRATE SPECIFICITY; SUBSTRATE-BINDING SITES;

HYDROLYSIS;

ADENOSINE PHOSPHATE; ALPHA,BETA METHYLENEADENOSINE DIPHOSPHATE; HISTIDINE; NUCLEOTIDE; PROTEIN SMPDL3A; SPHINGOMYELIN PHOSPHODIESTERASE; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; PROTEIN BINDING; SMPDL3A PROTEIN, MOUSE; ZINC;

ALPHA HELIX; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYMATIC ASSAY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; HYDROLYSIS KINETICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTON TRANSPORT; RESIDUE ANALYSIS; SEQUENCE ALIGNMENT; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; BIOCATALYSIS; CELL LINE; CHEMISTRY; HUMAN; HYDROLYSIS; KINETICS; MOLECULAR GENETICS; MOLECULAR MODEL; MOUSE; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ADENOSINE MONOPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BIOCATALYSIS; CATALYTIC DOMAIN; CELL LINE; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROLYSIS; KINETICS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SPHINGOMYELIN PHOSPHODIESTERASE; SUBSTRATE SPECIFICITY; ZINC;

EID: 84964709311     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.711085     Document Type: Article

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