O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding.
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The structure and function of proline-rich regions in proteinsGlycosylation variants of a β-glucosidase secreted by a Taiwanese fungus, Chaetomella raphigera, exhibit variant-specific catalytic and biochemical propertiesMass spectrometric identification of a stable catalytic cysteinesulfinic acid residue in an enzymatically active chemically modified glucoamylase mutant.Flux Design: In silico design of cell factories based on correlation of pathway fluxes to desired properties.Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism.Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domainsA novel endo-beta-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum.The carbohydrate-binding module family 20--diversity, structure, and function.Microbial glucoamylases: characteristics and applications.New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 alpha-amylase contributes to starch binding and raw starch degrading.Specificity of the binding domain of glucoamylase 1.Introduction of raw starch-binding domains into Bacillus subtilis alpha-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase.Comparative characterization of complete and truncated forms of Lactobacillus amylovorus alpha-amylase and role of the C-terminal direct repeats in raw-starch binding.Functional analysis of the threonine- and serine-rich Gp-I domain of glucoamylase I from Aspergillus awamori var. kawachiOverexpression of the gene encoding GTP:mannose-1-phosphate guanyltransferase, mpg1, increases cellular GDP-mannose levels and protein mannosylation in Trichoderma reesei.Streptomyces lividans glycosylates the linker region of a beta-1,4-glycanase from Cellulomonas fimi.Starch-binding domain affects catalysis in two Lactobacillus alpha-amylasesNovel characteristics of a carbohydrate-binding module 20 from hyperthermophilic bacterium.Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger.Cellulase production from spent lignocellulose hydrolysates by recombinant Aspergillus nigerTwo novel, putatively cell wall-associated and glycosylphosphatidylinositol-anchored alpha-glucanotransferase enzymes of Aspergillus nigerO-glycosylation and stability. Unfolding of glucoamylase induced by heat and guanidine hydrochloride.Expression in Aspergillus niger of the starch-binding domain of glucoamylase. Comparison with the proteolytically produced starch-binding domain.Glucoamylase structural, functional, and evolutionary relationships.The starch-binding domain from glucoamylase disrupts the structure of starch.Starch-binding domain of Aspergillus glucoamylase-I. Interaction with beta-cyclodextrin and maltoheptaose.
P2860
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P2860
O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh
1992年學術文章
@zh-hant
name
O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding.
@en
type
label
O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding.
@en
prefLabel
O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding.
@en
P2093
P2860
P356
P1433
P1476
O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding.
@en
P2093
Belshaw NJ
Williamson G
Williamson MP
P2860
P304
P356
10.1042/BJ2820423
P407
P478
282 ( Pt 2)
P577
1992-03-01T00:00:00Z