Two polymorphic forms of human histamine methyltransferase: Structural, thermal, and kinetic comparisons

Structure

Volumn 9, Issue 9, 2001, Pages 837-849

  Horton, John R ^a   Sawada, Ken ^a   Nishibori, Masahiro ^b   Zhang, Xing ^a   Cheng, Xiaodong ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b OKAYAMA UNIVERSITY MEDICAL SCHOOL   (Japan)

Author keywords

Antimalarial drug quinacrine; Histamine; Methylation; Polymorphism; Thermal stability

Indexed keywords

ANTIMALARIAL AGENT; ENZYME INHIBITOR; ENZYME VARIANT; HISTAMINE DERIVATIVE; HISTAMINE METHYLTRANSFERASE; ISOLEUCINE; MEPACRINE; RECOMBINANT ENZYME; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; THREONINE;

ALLELE; ARTICLE; BINDING SITE; COMPETITIVE INHIBITION; CONTROLLED STUDY; DISSOCIATION CONSTANT; DRUG PROTEIN BINDING; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITOR INTERACTION; ENZYME KINETICS; ENZYME POLYMORPHISM; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; HUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN VARIANT; STEADY STATE; STRUCTURE ANALYSIS; TEMPERATURE SENSITIVITY; THERMAL ANALYSIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ENZYME STABILITY; HISTAMINE; HISTAMINE N-METHYLTRANSFERASE; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYMORPHISM, GENETIC; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; QUINACRINE; RATS; S-ADENOSYLHOMOCYSTEINE; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; THERMODYNAMICS;

EID: 0034812118     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00643-8     Document Type: Article

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