1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family

Structure

Volumn 9, Issue 6, 2001, Pages 483-491

  Boltes, Imke ^a   Czapinska, Honorata ^a   Kahnert, Antje ^b   Von Bülow, Rixa ^a   Dierks, Thomas ^a   Schmidt, Bernhard ^a   Von Figura, Kurt ^a   Kertesz, Michael A ^b,c   Usón, Isabel ^a  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

^b ETH ZURICH   (Switzerland)

^c UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Catalytic mechanism; Crystal structure; Formylglycine hydrate; Multiple sulfatase deficiency (MSD); Sulfatase

Indexed keywords

4 NITROCATECHOLSULFATE; ARYLSULFATASE; CALCIUM; DIMER; FORMYLGLYCINE; GLYCINE DERIVATIVE; SULFATASE; SULFATE; UNCLASSIFIED DRUG; ESTER;

ARTICLE; ATOM; CATALYSIS; CHEMICAL BOND; CHEMICAL REACTION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; GEOMETRY; HYDRATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; PSEUDOMONAS AERUGINOSA; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYMOLOGY; HYDROLYSIS; METABOLISM; PROTEIN CONFORMATION;

BACTERIA (MICROORGANISMS); PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

ARYLSULFATASES; BINDING SITES; CATALYSIS; DIMERIZATION; ESTERS; HYDROLYSIS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PSEUDOMONAS AERUGINOSA; SULFATES;

EID: 0034987576     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00609-8     Document Type: Article

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