Mutational analysis of residues in the regulatory CBS domains of Moorella thermoacetica pyrophosphatase corresponding to disease-related residues of human proteins

Biochemical Journal

Volumn 433, Issue 3, 2011, Pages 497-504

  Jämsen, Joonas ^a   Tuominen, Heidi ^a   Baykov, Alexander A ^b   Lahti, Reijo ^a  

^a UNIVERSITY OF TURKU   (Finland)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Adenine nucleotide; Allosteric regulation; Cystathionine synthase domain (CBS domain); Inorganic pyrophosphatase; Moorella thermoacetica; Mutagenesis

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; ENZYME VARIANT; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; GENETIC SCREENING; MOORELLA THERMOACETICA; MUTATIONAL ANALYSIS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE ALIGNMENT; STOICHIOMETRY; WILD TYPE;

ADENOSINE MONOPHOSPHATE; AMINO ACID MOTIFS; BACTERIAL PROTEINS; CYSTATHIONINE BETA-SYNTHASE; DISEASE; DNA MUTATIONAL ANALYSIS; HUMANS; MOORELLA; MUTATION, MISSENSE; PROTEIN STRUCTURE, TERTIARY; PYROPHOSPHATASES;

BACTERIA (MICROORGANISMS); MOORELLA THERMOACETICA;

EID: 78751519886     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101204     Document Type: Article

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