Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease

FEBS Letters

Volumn 580, Issue 25, 2006, Pages 5899-5904

  Herga, S ^a   Berrin, J G ^a   Perrier, J ^a   Puigserver, A ^a   Giardina, T ^a  

^a AIX MARSEILLE UNIVERSITY   (France)

Author keywords

Aspartoacylase; Metalloenzyme; Molecular modelling; Site directed mutagenesis

Indexed keywords

ACETIC ACID; ASPARTOACYLASE; CARBOXYLIC ACID; CARBOXYPEPTIDASE; GLUTAMINE; HISTIDINE; HYDROGEN; LIGAND; METALLOPROTEIN; RECOMBINANT PROTEIN; ZINC;

ARTICLE; CANAVAN DISEASE; CATALYSIS; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME KINETICS; ESCHERICHIA COLI; HUMAN; LIGAND BINDING; MOLECULAR MODEL; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN MOTIF; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; WILD TYPE;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; CANAVAN DISEASE; CATALYTIC DOMAIN; DNA, COMPLEMENTARY; ESCHERICHIA COLI; GLUTAMIC ACID; HISTIDINE; HUMANS; KINETICS; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; ZINC;

ESCHERICHIA COLI;

EID: 33750996153     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.09.056     Document Type: Article

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