Mechanism of product specificity of AdoMet methylation catalyzed by lysine methyltransferases: Transcriptional factor p53 methylation by histone lysine methyltransferase SET7/9

Biochemistry

Volumn 47, Issue 9, 2008, Pages 2743-2748

  Zhang, Xiaodong ^a   Bruice, Thomas C ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL BONDS; FREE ENERGY; METHYLATION; MOLECULAR MECHANICS; QUANTUM THEORY;

ADOMET N-METHYLATION; BOND-ORDER COMPUTATIONS; ENERGY BARRIER; LYSINE METHYLTRANSFERASES;

ENZYMES;

AMIDE; AQUAPORIN; HISTONE LYSINE METHYLTRANSFERASE; METHIONINE; METHYL GROUP; PROTEIN P53; PROTON; S ADENOSYLMETHIONINE; SOLVENT;

AQUEOUS SOLUTION; ARTICLE; CALCULATION; CATALYSIS; CHEMICAL BOND; CHEMICAL REACTION; COMPLEX FORMATION; METHYLATION; MOLECULAR DYNAMICS; PRIORITY JOURNAL;

BINDING SITES; HISTONE-LYSINE N-METHYLTRANSFERASE; KINETICS; METHYLATION; MODELS, CHEMICAL; MOLECULAR STRUCTURE; SUBSTRATE SPECIFICITY; TUMOR SUPPRESSOR PROTEIN P53;

EID: 40149088321     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702370p     Document Type: Article

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