Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase.
about
Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteriaThe fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activityMutation of tyrosine167histidine at remote substrate binding subsite -6 in α-cyclodextrin glycosyltransferase enhancing α-cyclodextrin specificity by directed evolution.Enhancing the α-Cyclodextrin Specificity of Cyclodextrin Glycosyltransferase from Paenibacillus macerans by Mutagenesis Masking Subsite -7The evolution of cyclodextrin glucanotransferase product specificity.Iterative saturation mutagenesis of -6 subsite residues in cyclodextrin glycosyltransferase from Paenibacillus macerans to improve maltodextrin specificity for 2-O-D-glucopyranosyl-L-ascorbic acid synthesis.Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications.Evolution toward small molecule inhibitor resistance affects native enzyme function and stability, generating acarbose-insensitive cyclodextrin glucanotransferase variants.Molecular dynamic analysis of mutant Y195I α-cyclodextrin glycosyltransferase with switched product specificity from α-cyclodextrin to γ-cyclodextrin.Identification of the sequence motif of glycoside hydrolase 13 family members.Use of random and saturation mutageneses to improve the properties of Thermus aquaticus amylomaltase for efficient production of cycloamyloses.Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production.Decreasing the sialidase activity of multifunctional Pasteurella multocida α2-3-sialyltransferase 1 (PmST1) by site-directed mutagenesis.Hybrid reuteransucrase enzymes reveal regions important for glucosidic linkage specificity and the transglucosylation/hydrolysis ratio.Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.Semi-rational approach for converting a GH36 α-glycosidase into an α-transglycosidase.Improved activity of β-cyclodextrin glycosyltransferase from Bacillus sp. N-227 via mutagenesis of the conserved residues.
P2860
Q24544122-7A391905-2098-440A-A655-3567A6E2B710Q27641036-CE662862-0C71-4461-B57D-0BA5D9E0C34AQ34987546-CEDE185B-648E-47C8-880C-99B29F343838Q37122973-DA6A5D2E-13CC-42AD-B6EF-316075EF3D4BQ37271654-C7115FFE-F394-4EBA-812D-D3A097E5BEECQ37335533-42370784-A2EF-4488-8371-43C809481AFDQ37599536-E561929B-DB40-4A6C-8360-1F121834C340Q38293433-281C238C-90B0-461C-808E-658D8EB057EBQ38297385-31CFD119-79AA-462A-BB3A-5C752FCCA877Q41816689-13DF9264-8D13-4CED-898B-B009E8BAB466Q42122501-FFCAE258-FF5C-4010-BBFD-11A9058B5B80Q43015165-DEBFC612-1A78-4882-80FA-075CC82DD7E2Q43234776-B73EBE66-2B2B-4F59-B525-43B00643F0FBQ43765734-1A35BD3D-9FAB-440C-B00A-B001D226A65CQ46240076-0FC795F7-F712-4A31-8820-FF30459645C6Q48725453-D15CEB09-C70A-4794-B3C5-5C69057796E3Q51035435-AB11DBC4-BF95-4B41-B4C9-7704D3437623Q54877897-25B7DF4B-11B7-4F25-84BC-332E038B812C
P2860
Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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name
Mutations converting cyclodext ...... ylase into a starch hydrolase.
@en
Mutations converting cyclodext ...... ylase into a starch hydrolase.
@nl
type
label
Mutations converting cyclodext ...... ylase into a starch hydrolase.
@en
Mutations converting cyclodext ...... ylase into a starch hydrolase.
@nl
prefLabel
Mutations converting cyclodext ...... ylase into a starch hydrolase.
@en
Mutations converting cyclodext ...... ylase into a starch hydrolase.
@nl
P2860
P1433
P1476
Mutations converting cyclodext ...... ylase into a starch hydrolase.
@en
P2093
Bauke W Dijkstra
P2860
P304
P356
10.1016/S0014-5793(02)02362-1
P407
P577
2002-03-01T00:00:00Z