Regulation of S-adenosylhomocysteine hydrolase by lysine acetylation

Journal of Biological Chemistry

Volumn 289, Issue 45, 2014, Pages 31361-31372

  Wang, Yun ^a   Kavran, Jennifer M ^a   Chen, Zan ^a   Karukurichi, Kannan R ^a   Leahy, Daniel J ^a   Cole, Philip A ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

S-ADENOSYLHOMOCYSTEINE HYDROLASE;

ADENOSYLHOMOCYSTEINASE; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN BINDING; RECOMBINANT PROTEIN;

CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME REGULATION; ENZYME STRUCTURE; HUMAN; HYDROGEN BOND; NUCLEOTIDE BINDING SITE; NUCLEOTIDE SEQUENCE; PROTEIN ACETYLATION; PROTEIN FUNCTION; PROTEIN METHYLATION; PROTEIN MODIFICATION; REVIEW; X RAY CRYSTALLOGRAPHY; ACETYLATION; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; METABOLISM; METHYLATION; MOLECULAR GENETICS; PLASMID; PROTEIN PROCESSING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ACETYLATION; ADENOSYLHOMOCYSTEINASE; AMINO ACID SEQUENCE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROGEN BONDING; LYSINE; METHYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NAD; PLASMIDS; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84909957813     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.597153     Document Type: Review

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