About: Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases

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About: Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	wissenschaftlicher Artikel (de) artículu científicu espublizáu en 2007 (ast) наукова стаття, опублікована в березні 2007 (uk) 2007 թուականի Մարտին հրատարակուած գիտական յօդուած (hyw) 2007 թվականի մարտին հրատարակված գիտական հոդված (hy) wetenschappelijk artikel (gepubliceerd op 2007/03/20) (nl) مقالة علمية (نشرت في 20-3-2007) (ar) scientific journal article (en)
publication date	wds:Q28770305-238BCC6C-2AB3-4C82-9BAD-960FB6AF7727
publication date	2007-02-27 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28770305-52EC6168-6B36-4731-BD4A-D8FDAB412B2A
language of work or name	English
author name string	wds:Q28770305-46D7AB6C-A456-49EF-97CE-CBBCF6BA4622 wds:Q28770305-65C9C42B-48FC-446F-9838-9208EB97C484 wds:Q28770305-8F86A346-F26A-40B4-985F-194467C8D050 wds:Q28770305-C089D887-5FC5-43C4-ABA8-579AE590EE2E wds:Q28770305-E208919D-4E0D-465D-954A-8A3B07BC507B
OpenCitations bibliographic resource ID	wds:Q28770305-FE3C6776-9093-44EF-8626-5FB1AE17DD61
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/4781769
author name string	Harry Brumer Robert M Kelly James M Harris Kirill S Bobrov Dina R Ivanen
OpenCitations bibliographic resource ID	4781769
rdfs:label	Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases (en) Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases (ast)
skos:prefLabel	Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases (en) Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases (ast)
name	Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases (en) Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases (ast)
author	wds:Q28770305-22FE26A1-64F5-4221-99A0-ECD7DA118A8A wds:Q28770305-430EFAB6-31C5-41DF-A7CD-4506CA2F1434 wds:Q28770305-6840D32F-E29D-470D-99F7-E490187F4510
author	Anna Kulminskaya Konstantin Shabalin Donald A Comfort
title	wds:Q28770305-F10B36F8-EFBC-44D6-AD3C-4B148DE3B7B7
title	Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases (en)
page(s)	wds:Q28770305-218CCE52-C520-4954-ADCB-63F71B3293CF
page(s)	3319-3330
instance of	wds:Q28770305-89165BCA-CCF7-45EF-8A24-B477961CA919
instance of	scholarly article
main subject	wds:Q28770305-64F0E1C5-B7A7-45CF-91FF-548E9FB5A910 wds:Q28770305-8CFEA0E6-A298-4BA0-B050-09AD1F789044
main subject	Thermotoga maritima Thermotoga
PubMed ID	wds:Q28770305-315A8278-E90C-4753-9357-48078EE82BF8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17323919
PubMed ID	17323919
published in	wds:Q28770305-D68CEAA8-B774-47D3-92AF-E03BE0B23CEC
published in	Biochemistry
issue	wds:Q28770305-65CF1D8D-E674-49FA-ADE7-190145C0158C
volume	wds:Q28770305-B4ED799A-6CED-4DCA-BA77-12E1E70255E2
issue	11
volume	46
DOI	wds:Q28770305-4B395474-D192-40A3-A743-BF3EBE2E5614
DOI	http://dx.doi.org/10.1021/BI061521N
DOI	10.1021/BI061521N
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28770305
is cites work of	The Molecular Mechanism of Thermostable -Galactosidases AgaA and AgaB Explained by X-ray Crystallography and Mutational Studies Catalytic mechanism of human alpha-galactosidase Divergence of Catalytic Mechanism within a Glycosidase Family Provides Insight into Evolution of Carbohydrate Metabolism by Human Gut Flora α-N-acetylgalactosaminidase from infant-associated bifidobacteria belonging to novel glycoside hydrolase family 129 is implicated in alternative mucin degradation pathway Identification of a GH110 subfamily of alpha 1,3-galactosidases: novel enzymes for removal of the alpha 3Gal xenotransplantation antigen. α-Galactosidase/Sucrose Kinase (AgaSK), a Novel Bifunctional Enzyme from the Human Microbiome Coupling Galactosidase and Kinase Activities Biotechnological potential of microbial α-galactosidases Aspergillus nidulans alpha-galactosidase of glycoside hydrolase family 36 catalyses the formation of alpha-galacto-oligosaccharides by transglycosylation Molecular characterization and therapeutic potential of a marine bacterium Pseudoalteromonas sp. KMM 701 alpha-galactosidase. Functional analysis of family GH36 α-galactosidases from Ruminococcus gnavus E1: insights into the metabolism of a plant oligosaccharide by a human gut symbiont A novel α-galactosidase from the thermophilic probiotic Bacillus coagulans with remarkable protease-resistance and high hydrolytic activity. Exploitation of β-glycosyl azides for the preparation of α-glycosynthases A potent bicyclic inhibitor of a family 27 alpha-galactosidase. Insights into thermoadaptation and the evolution of mesophily from the bacterial phylum Thermotogae. Crystal Structure and Mutational Analysis of Isomalto-dextranase, a Member of Glycoside Hydrolase Family 27 An enzymatic pathway in the human gut microbiome that converts A to universal O type blood Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis. Probing the Catalytic Mechanism of Vibrio harveyi GH20 β-N-Acetylglucosaminidase by Chemical Rescue Raffinose family oligosaccharide utilisation by probiotic bacteria: insight into substrate recognition, molecular architecture and diversity of GH36 α-galactosidases Recombinant α-NAcetylgalactosaminidase from Marine Bacterium-Modifying A Erythrocyte Antigens Characterization of a long-chain α-galactosidase from Papiliotrema flavescens. Response surface methodology-based optimization of production media and purification of α-galactosidase in solid-state fermentation by Fusarium moniliforme NCIM 1099. Insights into the substrate specificity and synergy with mannanase of family 27 α-galactosidases from Neosartorya fischeri P1. A glycoside hydrolase family 31 dextranase with high transglucosylation activity from Flavobacterium johnsoniae. A new α-galactosidase from thermoacidophilic Alicyclobacillus sp. A4 with wide acceptor specificity for transglycosylation. The Effect of Fucoidan from the Brown Alga Fucus evanescence on the Activity of α-N-Acetylgalactosaminidase of Human Colon Carcinoma Cells. A β-mannan utilization locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans Hydrolysis of Oligosaccharides by a Thermostable α-Galactosidase from Termitomyces eurrhizus A mechanism-based inactivator of glycoside hydrolases involving formation of a transient non-classical carbocation Stereochemical course of hydrolytic reaction catalyzed by alpha-galactosidase from cold adaptable marine bacterium of genus Pseudoalteromonas. Characterization of Properties and Transglycosylation Abilities of Recombinant α-Galactosidase from Cold-Adapted Marine Bacterium KMM 701 and Its C494N and D451A Mutants Revealing the mechanism for covalent inhibition of glycoside hydrolases by carbasugars at an atomic level Enzymatic Conversion of RBCs by α-N-Acetylgalactosaminidase from Spirosoma linguale
is cites work of	wds:Q35643847-63BD5B0B-7768-4D44-9FAA-74414B231D17 wds:Q38128361-9329AC1A-C1CE-4FD6-8FA7-53D4C14C928C wds:Q54203097-2E4D5B96-7771-458B-8460-9CC168AD0E05 wds:Q58412972-4772F5F3-CD80-47B6-8827-34950BAFCF6F wds:Q27673640-CCA32CD3-FFF0-4519-B5A9-EF6BA23C4035 wds:Q39971624-E77DF6CC-AD9F-4BC0-8B68-97A64E2CDB81

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