Aromatic residues in the substrate cleft of RPE65 protein govern retinol isomerization and modulate its progression

Journal of Biological Chemistry

Volumn 287, Issue 36, 2012, Pages 30552-30559

  Chander, Preethi ^a   Gentleman, Susan ^a   Poliakov, Eugenia ^a   Redmond, T Michael ^a  

^a NATIONAL EYE INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACID PRODUCTS; AROMATIC RESIDUES; BINDING CLEFTS; CARBOCATIONS; DOCKING SIMULATIONS; INACTIVE ENZYMES; SUBSTRATE-BINDING; TEMPORAL SEQUENCES; VISUAL CYCLE;

AMINO ACIDS; ESTERIFICATION; ESTERS; ISOMERIZATION; SUBSTRATES;

ISOMERS;

HYDROLASE; PHENYLALANINE; RETINAL PIGMENT EPITHELIUM 65 PROTEIN; RETINOL; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CELL CULTURE; CELL STRAIN HEK293; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME SPECIFICITY; GENETIC TRANSFECTION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ISOMERIZATION; PRIORITY JOURNAL; SIMULATION; SITE DIRECTED MUTAGENESIS; WILD TYPE;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CIS-TRANS-ISOMERASES; CRYSTALLOGRAPHY, X-RAY; MICE; MUTATION, MISSENSE; PHENYLALANINE; PROTEIN BINDING; TYROSINE; VITAMIN A;

EID: 84865764391     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.364596     Document Type: Article

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