Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity
about
The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolutionThe remote substrate binding subsite -6 in cyclodextrin-glycosyltransferase controls the transferase activity of the enzyme via an induced-fit mechanismThe fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activityStructural Elucidation of the Cyclization Mechanism of -1,6-Glucan by Bacillus circulans T-3040 Cycloisomaltooligosaccharide GlucanotransferaseCrystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and productsThe raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1The functions of 4-alpha-glucanotransferases and their use for the production of cyclic glucans.Systems engineering of tyrosine 195, tyrosine 260, and glutamine 265 in cyclodextrin glycosyltransferase from Paenibacillus macerans to enhance maltodextrin specificity for 2-O-(D)-glucopyranosyl-(L)-ascorbic acid synthesisCarbohydrate-binding module-cyclodextrin glycosyltransferase fusion enables efficient synthesis of 2-O-d-glucopyranosyl-l-ascorbic acid with soluble starch as the glycosyl donor.The evolution of cyclodextrin glucanotransferase product specificity.The carbohydrate-binding module family 20--diversity, structure, and function.Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications.Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases.Strategies for enhancing extracellular secretion of recombinant cyclodextrin glucanotransferase in E. coli.Molecular dynamic analysis of mutant Y195I α-cyclodextrin glycosyltransferase with switched product specificity from α-cyclodextrin to γ-cyclodextrin.Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase.The role of arginine 47 in the cyclization and coupling reactions of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 implications for product inhibition and product specificity.The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms.Comparative study of the cyclization reactions of three bacterial cyclomaltodextrin glucanotransferases.Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50.A CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella.Use of random and saturation mutageneses to improve the properties of Thermus aquaticus amylomaltase for efficient production of cycloamyloses.Truncated human serum albumin retains general anaesthetic binding activity.Cyclodextrin glycosyltransferase: a key enzyme in the assimilation of starch by the halophilic archaeon Haloferax mediterranei.Site-saturation engineering of lysine 47 in cyclodextrin glycosyltransferase from Paenibacillus macerans to enhance substrate specificity towards maltodextrin for enzymatic synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid (AA-2G).Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase.Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase.CGTase-catalysed cis-glucosylation of L-rhamnosides for the preparation of Shigella flexneri 2a and 3a haptens.Improved activity of β-cyclodextrin glycosyltransferase from Bacillus sp. N-227 via mutagenesis of the conserved residues.
P2860
Q27620493-9512B489-05FD-418A-9CAE-4D9A9DF1E583Q27636015-B2B4ADDB-6FA1-4B73-BA76-0C09DB7E0899Q27641036-A05C7A23-9477-47E8-83D1-8C3F943A75ACQ27682073-5D0C81F0-B682-4435-9662-305C89607890Q27729318-C01DC5E2-2722-4A5E-9826-99C20BCAEE4FQ27734168-20B683B7-56D9-40DF-8C1B-264FB4827B7CQ27748894-66ADB6FA-1F64-4972-A8B6-20DD1413B541Q33923421-77FA4952-F57C-45F6-9708-BEF9448BDBECQ36558623-1E4C03F9-9B8B-4D82-9017-4056F8D21E99Q36936429-AE874E53-9F10-47EB-80FA-46743A31C31DQ37271654-D2DC0971-1D75-4440-A2EA-4EBCFC0E1638Q37580015-DE0E3330-8F0A-4F66-A5B8-1B3B81269BADQ37599536-A133CFE6-AA7A-47C1-BD30-7E8ABF13C5E4Q37895266-8B4389C2-A4E2-4E6A-AF78-DC2FF906336DQ38013737-FE6D9980-CD44-475D-9952-1DB7DF69056EQ38297385-7365EC61-02A7-4E49-87FE-FE0B64156FFFQ38302248-8112D165-1100-404C-BA6E-FD6D74EB2CF7Q38311498-62BF39A6-8CC3-4BE8-BC19-709102EB98C8Q38316000-24266E6F-9612-48B5-87B5-F9156E236399Q39490247-0577FB7F-D80C-48E4-9E83-F82F4A1FA131Q39504326-1DC964F4-9BC1-4AA1-BE8C-682370179476Q41684817-12C5CA17-0C35-4BEE-BDD9-1F5DE8C7C016Q42122501-9C286C09-DEAB-4852-BCF4-8DF577D972F7Q42936760-51D77A7C-46D9-40BB-9312-EF63AFB190F3Q43033681-FB9A570C-46BF-49D7-B953-3D7DDF773053Q43419382-10033981-977D-49CA-BEC3-6D97FA111C04Q43736489-1F6D396C-5623-44B5-88C5-1F394B7191CBQ43953801-CC3C4508-0621-4ACC-8CD1-23B5C08FD6B6Q54388156-732A3786-EE00-4098-B8C2-A45B0650AB81Q54877897-3F090134-37FB-4B87-B5AB-F6B352306D23
P2860
Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity
description
1995 nî lūn-bûn
@nan
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Site-directed mutations in tyr ...... tivity and product specificity
@ast
Site-directed mutations in tyr ...... tivity and product specificity
@en
Site-directed mutations in tyr ...... tivity and product specificity
@nl
type
label
Site-directed mutations in tyr ...... tivity and product specificity
@ast
Site-directed mutations in tyr ...... tivity and product specificity
@en
Site-directed mutations in tyr ...... tivity and product specificity
@nl
prefLabel
Site-directed mutations in tyr ...... tivity and product specificity
@ast
Site-directed mutations in tyr ...... tivity and product specificity
@en
Site-directed mutations in tyr ...... tivity and product specificity
@nl
P2093
P356
P1433
P1476
Site-directed mutations in tyr ...... tivity and product specificity
@en
P2093
B Strokopytov
B W Dijkstra
C L Lawson
D Penninga
H J Rozeboom
P304
P356
10.1021/BI00010A028
P407
P577
1995-03-14T00:00:00Z