A pathogenic linked mutation in the catalytic core of human cystathionine β-synthase disrupts allosteric regulation and allows kinetic characterization of a full-length dimer

Biochemistry

Volumn 46, Issue 13, 2007, Pages 4110-4116

  Sen, Suvajit ^a   Banerjee, Ruma ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHARACTERIZATION; ENZYMES; MIXTURES; OLIGOMERS; PATHOGENS; PURIFICATION; REACTION KINETICS;

CYSTATHIONINE; HOMOCYSTEINE; QUATERNARY STATES;

MUTAGENS;

CYSTATHIONINE BETA SYNTHASE; DEUTERIUM; HYDROGEN; S ADENOSYLMETHIONINE;

ALLOSTERISM; ARTICLE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME REGULATION; ENZYME SPECIFICITY; GENE LOCUS; GENE MUTATION; HOMOCYSTINURIA; HUMAN; HUMAN CELL; MASS SPECTROMETRY; OLIGOMERIZATION; POLYMERIZATION; PRIORITY JOURNAL; STEADY STATE;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CYSTATHIONINE BETA-SYNTHASE; DIMERIZATION; HOMOCYSTINURIA; HUMANS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; S-ADENOSYLMETHIONINE;

EID: 34047199341     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602617f     Document Type: Article

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