Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases.
about
Structure of the Arabidopsis Glucan Phosphatase LIKE SEX FOUR2 Reveals a Unique Mechanism for Starch DephosphorylationCrystal Structure of -1,4-Glucan Lyase, a Unique Glycoside Hydrolase Family Member with a Novel Catalytic MechanismCrystal Structure of the Chlamydomonas Starch Debranching Enzyme Isoamylase ISA1 Reveals Insights into the Mechanism of Branch Trimming and Complex AssemblyLigand Binding Enhances Millisecond Conformational Exchange in Xylanase B2 from Streptomyces lividansThe three Mycobacterium tuberculosis antigen 85 isoforms have unique substrates and activities determined by non-active site regions.Using Carbohydrate Interaction Assays to Reveal Novel Binding Sites in Carbohydrate Active Enzymes.Unique carbohydrate binding platforms employed by the glucan phosphatases.Structural mechanisms of plant glucan phosphatases in starch metabolismα-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Bound Substrate in the Structure of Cyanobacterial Branching Enzyme Supports a New Mechanistic Model.Learning from oligosaccharide soaks of crystals of an AA13 lytic polysaccharide monooxygenase: crystal packing, ligand binding and active-site disorder.Ligand-bound Structures and Site-directed Mutagenesis Identify the Acceptor and Secondary Binding Sites of Streptomyces coelicolor Maltosyltransferase GlgE.Expression and characterization of a Bifidobacterium adolescentis beta-mannanase carrying mannan-binding and cell association motifs.Structure and function of α-glucan debranching enzymes.Distribution of glucan-branching enzymes among prokaryotes.Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Characterization of surface binding sites in glycoside hydrolases: A computational study.Structural biology of glucan phosphatases from humans to plantsTransferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity.Isothermal titration calorimetry and surface plasmon resonance allow quantifying substrate binding to different binding sites of Bacillus subtilis xylanaseA new mechanism for starch dephosphorylation: insight from the structure of like sex four2.Arabidopsis β-Amylase2 Is a K+-Requiring, Catalytic Tetramer with Sigmoidal Kinetics.The Importance of Surface-Binding Site towards Starch-Adsorptivity Level in α-Amylase: A Review on Structural Point of View.Understanding the role of residues around the active site tunnel towards generating a glucose-tolerant β-glucosidase from Agrobacterium tumefaciens 5A.Sugar-coated sensor chip and nanoparticle surfaces for the in vitro enzymatic synthesis of starch-like materialsQuaternary Structure, Salt Sensitivity, and Allosteric Regulation of β-AMYLASE2 From
P2860
Q27678971-F03FEE4E-8516-4E1E-B88A-594E30033BA2Q27679302-0390F61C-5E3B-4DED-B4EA-2B016727D270Q27684546-0807E3E3-73AD-47CD-9BA5-281C1962F151Q27717116-21D97C2C-B6BF-42C7-8AF4-B9AF77059271Q34139044-6C53B98A-FEC4-4053-8A33-C570626B8105Q36098503-39C94B94-55F4-45D7-BD1D-8226E51679F4Q37037323-030F087B-B106-415A-83AC-AC2491B67016Q37072101-E494BF92-C7DA-4802-89D1-D1CD98F86098Q38117539-968F74C8-6661-475D-B64E-C50624ECDEFDQ38289061-57D8DC0E-6D0A-4203-8495-CBE9C815B5AAQ38289529-D16F7482-6084-4E85-9ED0-E7E1C4317E7CQ38291242-7958B91A-B428-4B35-B1E1-4F9567B895BDQ38320843-F3B7E583-F429-4967-93FA-2C4EAF162E59Q38823309-9C2A9D70-A96B-4738-9DFA-E4A6C319BBFDQ38824442-AE0AFFFD-3B4E-44E0-B4E1-ED9E4025FAB0Q38827804-BD05CD14-CFCA-4972-B5C3-BDF0F6D28BF2Q38906663-375DF1E3-7F1E-4422-AED8-11A4E949A696Q38920799-74E01256-8A9D-4E8C-9BD0-7EDC46ACE3DDQ40371311-F5DCF671-8524-476A-8036-6CF97F6116D0Q40911429-F30552C4-DB19-4CC2-BDCA-F64BC5C3EBB3Q44301821-95F66589-8B6E-4612-A399-8584392720DAQ45070927-0C0162D8-4A43-4E8B-B9F7-77A49C393CB4Q47557748-11B25724-D9A0-4AA5-AEE2-BF5F73AF64B1Q47713969-E283B73A-F9A0-4FFE-95FB-D11E2D62CF06Q57572152-DB3F2340-A23F-4A5A-8DAB-C1908ED6E395Q58781220-8F86C15B-3F86-4991-ACC2-E836B9FE0B50
P2860
Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 28 June 2011
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Occurrence and functional sign ...... sites in glycoside hydrolases.
@en
Occurrence and functional sign ...... sites in glycoside hydrolases.
@nl
type
label
Occurrence and functional sign ...... sites in glycoside hydrolases.
@en
Occurrence and functional sign ...... sites in glycoside hydrolases.
@nl
prefLabel
Occurrence and functional sign ...... sites in glycoside hydrolases.
@en
Occurrence and functional sign ...... sites in glycoside hydrolases.
@nl
P2093
P2860
P1476
Occurrence and functional sign ...... sites in glycoside hydrolases.
@en
P2093
Christophe M Courtin
Emmie Dornez
Jan A Delcour
Sven Cuyvers
P2860
P304
P356
10.3109/07388551.2011.561537
P577
2011-06-28T00:00:00Z