γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications

Cellular and Molecular Life Sciences

Volumn 69, Issue 20, 2012, Pages 3381-3394

  Castellano, Immacolata ^a   Merlino, Antonello ^b,c  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c CNR   (Italy)

Author keywords

Autoproteolytic activation; Biotechnological applications; Gamma glutamylhydrolase; Gamma glutamyltransferase; Gamma glutamyltranspeptidase; Glutathione

Indexed keywords

ACIVICIN; ANTINEOPLASTIC AGENT; BACTERIAL ENZYME; ENZYME INHIBITOR; GAMMA GLUTAMYLTRANSFERASE; GAMMA GLUTAMYLTRANSPEPTIDASE INHIBITOR; GLUTATHIONE; GLUTAURINE; HYDROXYL GROUP; LEVODOPA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; BETA SHEET; BINDING SITE; BIOCHEMISTRY; BIOTECHNOLOGY; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; FERMENTATION; GAMMA GLUTAMYL TRANSFERASE BLOOD LEVEL; GLUTATHIONE METABOLISM; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN GLYCOSYLATION; PROTEIN HYDROLYSIS; PROTEIN MODIFICATION; PROTEIN STRUCTURE; REVIEW; SALT TOLERANCE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; THERMOSTABILITY; TUBERCULOSIS;

AMINO ACID SEQUENCE; ANIMALS; BIOTECHNOLOGY; GAMMA-GLUTAMYLTRANSFERASE; GLUTAMINE; HUMANS; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84867576301     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-0988-3     Document Type: Review

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