Disruption of a calmodulin central helix-like region of 10-formyltetrahydrofolate dehydrogenase impairs its dehydrogenase activity by uncoupling the functional domains

Journal of Biological Chemistry

Volumn 278, Issue 25, 2003, Pages 22894-22900

  Reuland, Steven N ^b   Vlasov, Alexander P ^b   Krupenko, Sergey A ^a  

^a MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYST ACTIVITY; FLUORESCENCE; MOLECULAR STRUCTURE; MUTAGENESIS; NUCLEIC ACID SEQUENCES; SPECTROSCOPY;

CIRCULAR DICHROISM;

ENZYME KINETICS;

ALDEHYDE DEHYDROGENASE; CALMODULIN; DIHYDROFOLATE REDUCTASE; FORMATE TETRAHYDROFOLATE DEHYDROGENASE; HYDROLASE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CALMODULIN; CATALYTIC DOMAIN; CIRCULAR DICHROISM; CLONING, MOLECULAR; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; RESTRICTION MAPPING; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0038265173     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M302948200     Document Type: Article

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