Crystal Structures of the Catalytic Domain of a Novel Glycohydrolase Family 23 Chitinase fromRalstoniasp. A-471 Reveals a Unique Arrangement of the Catalytic Residues for Inverting Chitin Hydrolysis

Crystallization and preliminary X-ray diffraction studies of the catalytic domain of a novel chitinase, a member of GH family 23, from the moderately thermophilic bacteriumRalstoniasp. A-471

(2011) Nobuo Okazaki et al.   Acta Crystallographica Section F-Structural Biology and Crystallization Communications

Structural Relationships in the Lysozyme Superfamily: Significant Evidence for Glycoside Hydrolase Signature Motifs

(2010) Alexandre Wohlkönig et al.   PLoS One

Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism

(2009) Ronny Helland et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Mechanism of Cellulose Hydrolysis by Inverting GH8 Endoglucanases: A QM/MM Metadynamics Study

(2009) Luis Petersen et al.   JOURNAL OF PHYSICAL CHEMISTRY B

A novel goose-type lysozyme gene with chitinolytic activity from the moderately thermophilic bacterium Ralstonia sp. A-471: cloning, sequencing, and expression

(2008) Mitsuhiro Ueda et al.   APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

X-ray Structure of Papaya Chitinase Reveals the Substrate Binding Mode of Glycosyl Hydrolase Family 19 Chitinases†‡

(2008) Joëlle Huet et al.   BIOCHEMISTRY

The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics

(2008) B. L. Cantarel et al.   NUCLEIC ACIDS RESEARCH