CPL - Chalmers Publication Library
| Utbildning | Forskning | Styrkeområden | Om Chalmers | In English In English Ej inloggad.

Biochemical and Structural Characterization of a Five-domain GH115-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40(T)

W. J. Wang ; R. Y. Yan ; B. P. Nocek ; T. V. Vuong ; R. Di Leo ; X. H. Xu ; H. Cui ; Paul Gatenholm (Institutionen för kemi och kemiteknik, Polymerteknologi) ; Guillermo Toriz (Institutionen för kemi och kemiteknik, Polymerteknologi) ; M. Tenkanen ; A. Savchenko ; E. R. Master
Journal of Biological Chemistry (0021-9258). Vol. 291 (2016), 27, p. 14120-14133.
[Artikel, refereegranskad vetenskaplig]

Glucuronic acid (GlcAp) and/or methylglucuronic acid (MeGlcAp) decorate the major forms of xylan in hardwood and coniferous softwoods as well as many cereal grains. Accordingly, the complete utilization of glucuronoxylans or conversion to sugar precursors requires the action of main chain xylanases as well as -glucuronidases that release the - (12)-linked (Me)GlcAp side groups. Herein, a family GH115 enzymefrom the marine bacterium Saccharophagus degradans 2-40(T), SdeAgu115A, demonstrated activity toward glucuronoxylan and oligomers thereof with preference toward MeGlcAp linked to internal xylopyranosyl residues. Unique biochemical characteristics of NaCl activation were also observed. The crystal structure of SdeAgu115A revealed a five-domain architecture, with an additional insertion C+ domain that had significant impact on the domain arrangement of SdeAgu115A monomer and its dimerization. The participation of domain C+ in substrate binding was supported by reduced substrate inhibition upon introducing W773A, W689A, and F696A substitutions within this domain. In addition to Asp-335, the catalytic essentiality of Glu-216 was revealed by site-specific mutagenesis. A primary sequence analysis suggested that the SdeAgu115A architecture is shared by more than half of GH115 members, thus defining a distinct archetype for GH115 enzymes.

Nyckelord: carbohydrate, crystal structure, enzyme catalysis, enzyme structure, protein domain, GH115-glucuronidase, carbohydrate degradation, catalytic apparatus, enzyme domain composition, plant-cell wall, thermotoga-maritima msb8, alpha-glucuronidase, density, modification, family gh115, schizophyllum-commune, inverting character, crystal-structures, xylan, polysaccharides, Biochemistry & Molecular Biology, ruiter ga, 1992, analytical biochemistry, v207, p176

Denna post skapades 2016-08-23.
CPL Pubid: 240649


Läs direkt!

Länk till annan sajt (kan kräva inloggning)

Institutioner (Chalmers)

Institutionen för kemi och kemiteknik, Polymerteknologi


Biokemi och molekylärbiologi

Chalmers infrastruktur