Active site characterization of the exo-N-acetyl-β-d-glucosaminidase from thermotolerant Bacillus sp. NCIM 5120: involvement of tryptophan, histidine and carboxylate residues in catalytic activity-Reference-Cited by-同舟云学术

Active site characterization of the exo-N-acetyl-β-d-glucosaminidase from thermotolerant Bacillus sp. NCIM 5120: involvement of tryptophan, histidine and carboxylate residues in catalytic activity

Published:1999-03 Issue:1 Volume:1427 Page:121-132
ISSN:0304-4165
Container-title:Biochimica et Biophysica Acta (BBA) - General Subjects
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - General Subjects

Author:

Amutha Boominathan,Khire Jayant M,Khan M.Islam

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference27 articles.

1. Updating the sequence-based classification of glycosyl hydrolases

2. Natural History and Inherited Disorders of a Lysosomal Enzyme, β-Hexosaminidase

3. Structures and mechanisms of glycosyl hydrolases

4. Mechanism of catalysis by retaining β-glycosyl hydrolases

5. Active arginine residues in beta-hexosaminidase. Identification through studies of the B1 variant of Tay-Sachs disease

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