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Biochemical and Str...
Biochemical and Structural Characterization of a Five-domain GH115-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40(T)
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- Wang, W. J. (författare)
- University of Toronto
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- Yan, R. Y. (författare)
- University of Toronto
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- Nocek, B. P. (författare)
- Argonne National Laboratory
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visa fler...
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- Vuong, T. V. (författare)
- University of Toronto
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- Di Leo, R. (författare)
- University of Toronto
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- Xu, X. H. (författare)
- University of Toronto
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- Cui, H. (författare)
- University of Toronto
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- Gatenholm, Paul, 1956 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Toriz Gonzalez, Guillermo, 1968 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Tenkanen, M. (författare)
- Helsingin Yliopisto,University of Helsinki
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- Savchenko, A. (författare)
- University of Toronto
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Master, E. R. (författare)
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(creator_code:org_t)
- 2016
- 2016
- Engelska.
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 291:27, s. 14120-14133
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https://research.cha... (primary) (free)
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- crystal structure
- protein domain
- enzyme domain composition
- carbohydrate degradation
- enzyme catalysis
- enzyme structure
- GH115-glucuronidase
- carbohydrate
- catalytic apparatus
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Wang, W. J.
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Yan, R. Y.
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Nocek, B. P.
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Vuong, T. V.
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Di Leo, R.
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Xu, X. H.
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visa fler...
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Cui, H.
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Gatenholm, Paul, ...
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Toriz Gonzalez, ...
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Tenkanen, M.
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Savchenko, A.
-
Master, E. R.
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visa färre...
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