Amino acid residues crucial in pH regulation and proteolytic activation of N-acylethanolamine-hydrolyzing acid amidase

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1781, Issue 11-12, 2008, Pages 710-717

  Wang, Jun ^a,b   Zhao, Li Ying ^a,b   Uyama, Toru ^a   Tsuboi, Kazuhito ^a   Tonai, Takeharu ^c   Ueda, Natsuo ^a  

^a KAGAWA UNIVERSITY   (Japan)

^b CHINA MEDICAL UNIVERSITY   (China)

^c National Hospital Organization   (Japan)

Author keywords

Acidic pH optimum; Anandamide; Endocannabinoid; Lysosomal enzyme; Ntn hydrolase family

Indexed keywords

AMINO ACID; ARGININE; ASPARAGINE; ASPARTIC ACID; CONCANAMYCIN A; CYSTEINE; GLUTAMIC ACID; LYSOSOME ENZYME; PALMIDROL;

ARTICLE; CATALYSIS; CELL MATURATION; CELL STRAIN HEK293; ENZYME ACTIVITY; HUMAN; HUMAN CELL; HYDROLYSIS; HYDROLYSIS KINETICS; KIDNEY CELL; LYSOSOME; PH; PRECURSOR; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS;

ACID CERAMIDASE; AMIDOHYDROLASES; AMINO ACID SEQUENCE; AMINO ACIDS; AMMONIUM CHLORIDE; BLOTTING, WESTERN; CELLS, CULTURED; ENZYME ACTIVATION; GLUTAMIC ACID; GLYCOSYLATION; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KIDNEY; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE HYDROLASES; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 56049109746     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2008.08.004     Document Type: Article

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