Negative charge of the glutamic acid 417 residue is crucial for isomerohydrolase activity of RPE65

Biochemical and Biophysical Research Communications

Volumn 391, Issue 4, 2010, Pages 1757-1761

  Nikolaeva, Olga ^a   Takahashi, Yusuke ^a   Moiseyev, Gennadiy ^a   Ma, Jian xing ^a  

^a UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

Author keywords

Isomerohydrolase; Leber congenital amaurosis; Retinoids; RPE65; Visual cycle

Indexed keywords

GLUTAMIC ACID; HYDROLASE; ISOMEROHYDROLASE; MUTANT PROTEIN; PROTEIN RPE65; UNCLASSIFIED DRUG;

ARTICLE; BLINDNESS; CATALYSIS; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ENZYME ACTIVITY; GENE MUTATION; HUMAN; HUMAN CELL; LEBER CONGENITAL AMAUROSIS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN STABILITY; WILD TYPE;

BLINDNESS; CARRIER PROTEINS; CIS-TRANS-ISOMERASES; EYE PROTEINS; GLUTAMIC ACID; HUMANS; LEBER CONGENITAL AMAUROSIS; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; STATIC ELECTRICITY;

EID: 74449085914     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.12.149     Document Type: Article

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