Intramolecular disulfide bonds are required for folding hydrolase B into a catalytically active conformation but not for maintaining it during catalysis

Biochemical and Biophysical Research Communications

Volumn 319, Issue 4, 2004, Pages 1072-1080

  Song, Xiulong ^a   Gragen, Sarah ^a   Li, Yuxin ^a   Ma, Yuzhong ^a   Liu, Jirong ^a   Yang, Dongfang ^a   Matoney, Lynn ^a   Yan, Bingfang ^a  

^a UNIVERSITY OF RHODE ISLAND   (United States)

Author keywords

Carboxylesterase; Disulfide bond; Esterase; Folding; Hydrolase B; Lipase

Indexed keywords

HYDROLASE;

ANIMAL CELL; ARTICLE; CATALYSIS; CHEMICAL BOND; CONTROLLED STUDY; ELECTROPHORESIS; ENZYME DEGRADATION; HUMAN; HUMAN CELL; MICROSOME; NONHUMAN; PRIORITY JOURNAL; REDUCTION;

ANIMALS; CARBOXYLESTERASE; CARBOXYLIC ESTER HYDROLASES; CYSTEINE; DISULFIDES; DITHIOTHREITOL; MICROSOMES, LIVER; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RATS; UREA;

EID: 2942603512     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.090     Document Type: Article

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