Multidomain structure and cellulosomal localization of the Clostridium thermocellum cellobiohydrolase CbhA.
about
Cellulase, clostridia, and ethanol.Microbial cellulose utilization: fundamentals and biotechnologyModeling the self-assembly of the cellulosome enzyme complex.Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to celluloseCelE, a multidomain cellulase from Clostridium cellulolyticum: a key enzyme in the cellulosome?EndB, a multidomain family 44 cellulase from Ruminococcus flavefaciens 17, binds to cellulose via a novel cellulose-binding module and to another R. flavefaciens protein via a dockerin domain.Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: evidence for gene duplication and recombination.The fibronectin type 3-like repeat from the Clostridium thermocellum cellobiohydrolase CbhA promotes hydrolysis of cellulose by modifying its surface.Ruminococcus albus 8 mutants defective in cellulose degradation are deficient in two processive endocellulases, Cel48A and Cel9B, both of which possess a novel modular architectureComplete cellulase system in the marine bacterium Saccharophagus degradans strain 2-40T.Enzymatic diversity of the Clostridium thermocellum cellulosome is crucial for the degradation of crystalline cellulose and plant biomass.Advances in development of a genetic system for Thermoanaerobacterium spp.: expression of genes encoding hydrolytic enzymes, development of a second shuttle vector, and integration of genes into the chromosome.Properties and mutation analysis of the CelK cellulose-binding domain from the Clostridium thermocellum cellulosome.Hydrophilic domains of scaffolding protein CbpA promote glycosyl hydrolase activity and localization of cellulosomes to the cell surface of Clostridium cellulovoransMultiple cellobiohydrolases and cellobiose phosphorylases cooperate in the ruminal bacterium Ruminococcus albus 8 to degrade cellooligosaccharides.Global view of the Clostridium thermocellum cellulosome revealed by quantitative proteomic analysis.Calcium and domain interactions contribute to the thermostability of domains of the multimodular cellobiohydrolase, CbhA, a subunit of the Clostridium thermocellum cellulosomeComparative characterization of all cellulosomal cellulases from Clostridium thermocellum reveals high diversity in endoglucanase product formation essential for complex activityNovel Insights from Comparative In Silico Analysis of Green Microalgal Cellulases.Optimizing the composition of a synthetic cellulosome complex for the hydrolysis of softwood pulp: identification of the enzymatic core functions and biochemical complex characterization
P2860
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P2860
Multidomain structure and cellulosomal localization of the Clostridium thermocellum cellobiohydrolase CbhA.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Multidomain structure and cell ...... cellum cellobiohydrolase CbhA.
@ast
Multidomain structure and cell ...... cellum cellobiohydrolase CbhA.
@en
type
label
Multidomain structure and cell ...... cellum cellobiohydrolase CbhA.
@ast
Multidomain structure and cell ...... cellum cellobiohydrolase CbhA.
@en
prefLabel
Multidomain structure and cell ...... cellum cellobiohydrolase CbhA.
@ast
Multidomain structure and cell ...... cellum cellobiohydrolase CbhA.
@en
P2093
P2860
P1476
Multidomain structure and cell ...... cellum cellobiohydrolase CbhA.
@en
P2093
G V Velikodvorskaya
J Kellermann
K Bronnenmeier
V V Zverlov
W H Schwarz
W L Staudenbauer
P2860
P304
P407
P577
1998-06-01T00:00:00Z