Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase.

Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase.

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http://www.wikidata.org/entity/Q38302248
The remote substrate binding subsite -6 in cyclodextrin-glycosyltransferase controls the transferase activity of the enzyme via an induced-fit mechanismCrystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitorRole of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic siteThermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formedThe 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.Molecular dynamic analysis of mutant Y195I α-cyclodextrin glycosyltransferase with switched product specificity from α-cyclodextrin to γ-cyclodextrin.Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley alpha-amylase 1.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.Kinetics of cytochrome C folding: atomically detailed simulations.Purification and characterization of cyclic maltosyl-(1-->6)-maltose hydrolase and alpha-glucosidase from an Arthrobacter globiformis strain.Structural features of a bacterial cyclic α-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis
P2860

Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase.

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http://www.wikidata.org/entity/Q38302248
description
2001 nî lūn-bûn
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2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Enzymatic circularization of a ...... lodextrin glycosyltransferase.
@en
type
label
Enzymatic circularization of a ...... lodextrin glycosyltransferase.
@en
prefLabel
Enzymatic circularization of a ...... lodextrin glycosyltransferase.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
Enzymatic circularization of a ...... lodextrin glycosyltransferase.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698