Probing the role of an invariant active site His in family GH1 β-glycosidases-Reference-Cited by-同舟云学术

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Probing the role of an invariant active site His in family GH1 β-glycosidases

Published:2019-01-01 Issue:1 Volume:34 Page:973-980
ISSN:1475-6366
Container-title:Journal of Enzyme Inhibition and Medicinal Chemistry
language:en
Short-container-title:Journal of Enzyme Inhibition and Medicinal Chemistry

Author:

Strazzulli Andrea¹²^ORCID,Perugino Giuseppe³^ORCID,Mazzone Marialuisa³,Rossi Mosè³,Withers Stephen G.⁴,Moracci Marco¹²³^ORCID

Affiliation:

1. Department of Biology, University of Naples "Federico II", Complesso Universitario di Monte S. Angelo, Napoli, Italy;

2. Task Force on Microbiome Studies, University of Naples Federico II, Naples, Italy;

3. Institute of Biosciences and BioResources – National Research Council of Italy, Naples, Italy;

4. Department of Chemistry, University of British Columbia, Vancouver, Canada

Publisher

Informa UK Limited

Subject

Drug Discovery,Pharmacology,General Medicine

Link

https://tandfonline.com/doi/pdf/10.1080/14756366.2019.1608198

Reference43 articles.

1. The carbohydrate-active enzymes database (CAZy) in 2013

2. Expression and extensive characterization of a β-glycosidase from the extreme thermoacidophilic archaeon Sulfolobus solfataricus in Escherichia coli: Authenticity of the recombinant enzyme

3. Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats

4. BIOLOGY AND BIOCHEMISTRY OF GLUCOSINOLATES

5. Lactose malabsorption and intolerance: a review

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1. Dried tea residue can alter the blood metabolism and the composition and functionality of the intestinal microbiota in Hu sheep;Frontiers in Microbiology;2023-11-03

2. Molecular and biochemical characterization of a recombinant glycosyl hydrolase family 3 β-glucosidase overexpressed in Escherichia. coli; bioprospecting metagenomes for cellulolytic processing function;Molecular Catalysis;2023-05

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