The X-ray Crystal Structure of an Arthrobacter protophormiae Endo-β-N-Acetylglucosaminidase Reveals a (β/α)8 Catalytic Domain, Two Ancillary Domains and Active Site Residues Key for Transglycosylation Activity

Journal of Molecular Biology

Volumn 389, Issue 1, 2009, Pages 1-9

  Ling, Zhenlian ^a   Suits, Michel D L ^a   Bingham, Richard J ^a   Bruce, Neil C ^a   Davies, Gideon J ^a   Fairbanks, Antony J ^b   Moir, James W B ^a   Taylor, Edward J ^a  

^a UNIVERSITY OF YORK   (United Kingdom)

^b UNIVERSITY OF CANTERBURY   (New Zealand)

Author keywords

EC 3.2.1.96; glycoside hydrolase; substrate assisted catalysis; transglycosylase endo N acetylglucosaminidase; X ray structure

Indexed keywords

ASPARAGINE; ASPARTIC ACID; GLUTAMIC ACID; GLYCOPROTEIN; GLYCOSIDASE; MUTANT PROTEIN; N ACETYL BETA GLUCOSAMINIDASE; OXAZOLINE DERIVATIVE;

ARTHROBACTER; ARTHROBACTER PROTOPHORMIAE; ARTICLE; BETA SHEET; BIOCATALYST; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GLYCOSYLATION; MOLECULAR IMAGING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN VARIANT; X RAY CRYSTALLOGRAPHY;

ARTHROBACTER PROTOPHORMIAE;

EID: 67349093886     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.03.050     Document Type: Article

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