Rat liver betaine-homocysteine S-methyltransferase equilibrium unfolding: Insights into intermediate structure through tryptophan substitutions

Biochemical Journal

Volumn 391, Issue 3, 2005, Pages 589-599

  Garrido, Francisco ^a   Gasset, María ^b   Sanz Aparicio, Juliana ^b   Alfonso, Carlos ^c   Pajares, Maria A ^a  

^a INSTITUTO DE INVESTIGACIONES BIOMÉDICAS ALBERTO SOLS   (Spain)

^b INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^c CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

Author keywords

Betaine homocysteine methyltransferase folding; Monomeric intermediate; Tetrameric intermediate; Triosephosphate isomerase (TIM) barrel; Tryptophan fluorescence

Indexed keywords

ACTIVATION ENERGY; DISSOCIATION; ENZYMES; FLUORESCENCE; MONOMERS;

BETAINE-HOMOCYSTEINE METHYLTRASFERASE FOLDING; MONOMERIC INTERMEDIATE; TETRAMERIC INTERMEDIATE; TRIOSEPHOSPHATE ISOMERASE (TIM) BARREL; TRYPTOPHAN FLUORESCENCE;

BIOLOGICAL ORGANS;

BETAINE HOMOCYSTEINE METHYLTRANSFERASE; TRYPTOPHAN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; RAT; SEDIMENTATION;

AMINO ACID SUBSTITUTION; ANIMALS; BETAINE-HOMOCYSTEINE S-METHYLTRANSFERASE; GENE EXPRESSION REGULATION; LIVER; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RATS; TRYPTOPHAN;

ANIMALIA;

EID: 27744488576     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050505     Document Type: Article

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