About: Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii

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About: Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii Goto Sponge NotDistinct Permalink

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scientific article published on 01 February 1981

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 1981 (uk) artículu científicu espublizáu en febreru de 1981 (ast) scientific article published on 01 February 1981 (en) im Februar 1981 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q71541016-6122FBD0-AB2B-4CC5-B748-2700C87A008B
publication date	1981-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71541016-EA62F5B4-4204-42FD-A674-F47610D559D3
language of work or name	English
author name string	wds:Q71541016-624F22E2-9C1F-4F30-BFE4-AE42788DB93B wds:Q71541016-A38F4C2B-6550-4AAB-B7E6-B7934B58DC26
author name string	G Legler K R Roeser
rdfs:label	Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (en) Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (nl) Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (sq)
skos:prefLabel	Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (en) Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (nl) Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (sq)
name	Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (en) Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (nl) Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (sq)
title	wds:Q71541016-A98FFE5E-D1FC-43E4-8244-DBFB4DE591B1
title	Role of sugar hydroxyl groups in glycoside hydrolysis. Cleavage mechanism of deoxyglucosides and related substrates by beta-glucosidase A3 from Aspergillus wentii (en)
page(s)	wds:Q71541016-6D3F0E48-4843-47FF-BD71-C3250ACE2E98
page(s)	321-333
instance of	wds:Q71541016-885D33B6-6728-48F4-B789-11AD1A8F60E7
instance of	scholarly article
main subject	wds:Q71541016-937F6C7B-EE6C-4C89-863A-7D9B288C7F89
main subject	Aspergillus wentii
PubMed ID	wds:Q71541016-1E8FAF17-3A3C-4CA1-9FEC-37CE6764EB99
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6783098
PubMed ID	6783098
published in	wds:Q71541016-E413EE46-F121-4A87-A399-0F862E381105
published in	Biochimica et Biophysica Acta
issue	wds:Q71541016-3BF8FE61-B5D8-4478-B84C-F51FC9BE5A91
volume	wds:Q71541016-82CC63DE-75DA-4BB7-B5C0-9BDC21D95840
issue	2
volume	657
number of pages	wds:Q71541016-FFB7D359-A8C5-465A-AF3E-F50B32CCECAB
number of pages	13 (xsd:decimal)
DOI	wds:Q71541016-50441398-6629-4C3D-8AB2-65E5D6F1E3D0
DOI	http://dx.doi.org/10.1016/0005-2744(81)90318-1
DOI	10.1016/0005-2744(81)90318-1
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71541016
is cites work of	Dissecting conformational contributions to glycosidase catalysis and inhibition Binding energy and catalysis. Fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lacZ) beta-galactosidase Active site-directed inhibition of galactosidases by conduritol C epoxides (1,2-anhydro-EPI -and NEO -inositol Approaches to labeling and identification of active site residues in glycosidases Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase Mechanism of catalysis by retaining beta-glycosyl hydrolases Biological evaluation of a series of 2-acetamido-2-deoxy-D-glucose analogs towards cellular glycosaminoglycan and protein synthesis in vitro Synthesis of 4-deoxy-4-fluoro analogues of 2-acetamido-2-deoxy-D-glucose and 2-acetamido-2-deoxy-D-galactose and their effects on cellular glycosaminoglycan biosynthesis Functional proteomic profiling of glycan-processing enzymes The use of inhibitors in the study of glycosidases Synthesis of 5-amino-5-deoxy-d-mannopyranose and 1,5-di-deoxy-1,5-imino-d-mannitol, and inhibition of α- and β-d-mannosidases Paenibacillus sp. TS12 glucosylceramidase: kinetic studies of a novel sub-family of family 3 glycosidases and identification of the catalytic residues Subsite structure of the beta-glucosidase from Aspergillus niger, evaluated by steady-state kinetics with cello-oligosaccharides as substrates Hydrolytic activity of alpha-galactosidases against deoxy derivatives of p-nitrophenyl alpha-D-galactopyranoside. Synthesis of 5-amino-5-deoxy-D-galactopyranose and 1,5-dideoxy-1,5-imino-D-galactitol, and their inhibition of alpha- and beta-D-galactosidases Glycon specificity profiling of alpha-glucosidases using monodeoxy and mono-O-methyl derivatives of p-nitrophenyl alpha-D-glucopyranoside Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human -GlcNAcase Comparative stability of 1-alkoxyalkyl alpha-D-glucosides in the presence of acid or alpha-D-glucosidase from yeast N1-alkyl-D-gluconamidines: are they 'perfect' mimics of the first transition state of glucosidase action? [Sugar analog inhibitors for glycosidases, tools for the elucidation of enzymatic hydrolysis of glycosides]
is cites work of	wds:Q36658525-EBDDDBF7-734C-4CF1-86FD-1C41863C7EE8 wds:Q38348340-0202960E-755F-4DF9-AE69-60A78A69674F wds:Q41622317-DF6BC0CA-B0DE-427F-AF1D-96715EF23F80 wds:Q42156948-83EED5FA-1489-486C-8A29-97BDDC6186B1 wds:Q46823604-CF4CC4D0-F5F3-4038-AC2C-861D445686D3 wds:Q70156801-EF35700F-3EA8-448E-B8E9-5B796C1CBCCC wds:Q27732530-02C45275-C610-4F62-8BA4-A30CF797E080 wds:Q36279056-72D8EF5B-74EF-4024-BEA8-5E0D709E2ADD wds:Q41822034-C5D5E14A-8694-4535-9FBD-B280C4BED48A wds:Q72817419-F15AC40B-E7E1-44E6-9979-2FB214CEB076 wds:Q38228725-0A14BFEB-B0F5-43E1-AF2F-DD5CD7AC6692 wds:Q43927954-ECBF2A3C-9FA6-47B0-8F8C-B02FED918F4F wds:Q64933825-64933B5B-F8E4-4828-9FDC-B92EEC3DB0C5 wds:Q57810292-C86675FC-448B-478D-A0B7-F3D0E833C391 wds:Q72917696-C4C71B62-E2F8-4462-BD03-6B30B83D43DE wds:Q43504966-FF34EF16-B4CC-409F-8CD6-3F344EB36501 wds:Q42225485-FA520E67-1159-4E97-A03E-68B32F435707 wds:Q71684291-94F6BC1E-D5F4-49CE-AF5F-336C54E8D822 wds:Q40267405-3902DF77-ED72-460B-AFEB-E43E54420A36 wds:Q70513876-80A48E65-04D4-4F16-B5CD-02D2FE37D125

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