Investigation of the active site of the extracellular β-D-glucosidase from Aspergillus carbonarius
Author:
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Physiology,Biotechnology
Link
http://link.springer.com/content/pdf/10.1007/s11274-004-2609-2.pdf
Reference36 articles.
1. 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
2. The Glu residue in the conserved ASN-Glu-Pro sequence of two highly divergent endo-β-1,4-glucanases is essential for enzymatic activity
3. N-Bromoacetyl-glycopyranosylamines as affinity labels for a β-glucosidase and a cellulase
4. Ethanol Production from Agricultural Biomass Substrates
5. Essential carboxy groups in xylanase A
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1. Orthogonal Active-Site Labels for Mixed-Linkage endo-β-Glucanases;ACS Chemical Biology;2021-05-14
2. The geochemical evaluation and biological effect of Aspergillus niger on the kerogen-bearing limestone of El Galala El Qebbliay plateau, Wadi Araba area, North Eastern Desert, Egypt;Egyptian Journal of Petroleum;2017-09
3. A New Approach in the Active Site Investigation of an Inverting β-d-Xylosidase from Thermobifida fusca TM51;The Protein Journal;2013-01-19
4. Suite of Activity-Based Probes for Cellulose-Degrading Enzymes;Journal of the American Chemical Society;2012-12-06
5. Purification and some properties of endoglucanase from Glyptotermes xiamenensis;Journal of Applied Entomology;2010-11-10
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