Functional and structural properties of a novel cellulosome-like multienzyme complex: efficient glycoside hydrolysis of water-insoluble 7-xylosyl-10-deacetylpaclitaxel.
Sci Rep, 2015/9/08;5:13768.
Dou TY[1, 2], Luan HW[1], Ge GB[1], Dong MM[3], Zou HF[3], He YQ[1], Cui P[1, 2], Wang JY[1, 2], Hao DC[4], Yang SL[5], Yang L[1, 5]
Affiliations
PMID: 26347949DOI: 10.1038/srep13768
Impact factor: 4.996
Abstract
Cellulosome is a kind of multienzyme complex that displays high activity, selectivity, and stability. Here, we report a novel, non-cellulolytic, cellulosome-like multienzyme complex that produced by the Cellulosimicrobium cellulans wild-type strain F16 isolated from soil microflora. This multienzyme complex, with excellent catalytic efficiency of kcat 13.2 s(-1) to remove the C-7 xylosyl group from 7-xylosyl-10-deacetylpaclitaxel (10-DAXP), has an outstanding tolerance against organic solvents and an excellent general stability, with the long half-life of 214 hours. This cellulosome-like multienzyme complex has a novel structure distinct from the well-documented ones. The key catalytic subunit responsible for the β-xylosidase activity against 10-DAXP is identified to be a novel protein, indicating a new glycoside hydrolase (GH) family. The pioneering work described here offers a novel nanoscale biocatalyst for the production of biofuels and chemicals from renewable plant-based natural resources.
MeSH terms
Amino Acid Sequence; Catalysis; Cellulosomes; Enzyme Activation; Enzyme Stability; Genome, Bacterial; Genomics; Glycosides; High-Throughput Nucleotide Sequencing; Hydrolysis; Kinetics; Molecular Sequence Data; Multienzyme Complexes; Paclitaxel; Protein Structure, Secondary; Protein Subunits; Sequence Alignment; Structure-Activity Relationship; Substrate Specificity
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