uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Three-dimensional Crystal Structure and Enzymic Characterization of β-Mannanase Man5A from Blue Mussel Mytilus edulis
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
Show others and affiliations
2006 (English)In: Journal of Molecular Biology, Vol. 357, no 5, 1500-1510 p.Article in journal (Refereed) Published
Description
Abstract [en]

Endo-β-1,4-d-mannanase is the key depolymerizing enzyme for β-1,4-mannan polymers present in the cell walls of plants and some algae, as well as in some types of plant seeds. Endo-1,4-β-mannanase from blue mussel Mytilus edulis (MeMan5A) belongs to the glycoside hydrolase (GH) family 5 enzymes. The MeMan5A structure has been determined to 1.6 resolution using the multiple-wavelength anomalous dispersion method at the selenium K edge with selenomethionyl MeMan5A expressed in the yeast Pichia pastoris. As expected for GH 5 enzymes, the structure showed a (βα)8-barrel fold. An unusually large number of histidine side-chains are exposed on the surface, which may relate to its location within the crystalline style of the digestive tract of the mussel. Kinetic analysis of MeMan5A revealed that the enzyme requires at least six subsites for efficient hydrolysis. Mannotetraose (M4) and mannopentaose (M5) were shown to interact with subsites −3 to +1, and −3 to +2, respectively. A clear kinetic threshold was observed when going from M4 to M5, indicating that the +2 subsite provides important interaction in the hydrolysis of short oligomeric mannose substrates. The catalytic centre motif at subsite −1 found in superfamily GH clan A is, as expected, conserved in MeMan5A, but the architecture of the catalytic cleft differs significantly from other GH 5 enzyme structures. We therefore suggest that MeMan5A represents a new subfamily in GH 5.

Place, publisher, year, edition, pages
2006. Vol. 357, no 5, 1500-1510 p.
Keyword [en]
mannanase, Mytilus edulis, SeMet, Pichia pastoris, MAD
Identifiers
URN: urn:nbn:se:uu:diva-77532OAI: oai:DiVA.org:uu-77532DiVA: diva2:105444
Available from: 2007-02-13 Created: 2007-02-13 Last updated: 2016-05-12

Open Access in DiVA

No full text

Other links

http://www.sciencedirect.com/science?_ob=ArticleURL&_aset=V-WA-A-W-V-MsSAYZA-UUW-U-AAVCUUBYVZ-AAVWCYVZVZ-DWZWDZDDB-V-U&_rdoc=1&_fmt=full&_udi=B6WK7-4J5D6HH-5&_coverDate=01%2F31%2F2006&_cdi=6899&_orig=search&_st=13&_sort=d&view=c&_acct=C000035158&_version=1&_urlVersion=0&_userid=651519&md5=77e07835394a564a2bbc9303911fa1d8

Authority records BETA

Larsson, Anna M.Janson, Jan-Christer

Search in DiVA

By author/editor
Larsson, Anna M.Janson, Jan-Christer
By organisation
Department of Cell and Molecular BiologySurface BiotechnologyDepartment of Biochemistry and Organic ChemistrySurface BiotechnologyDepartment of Physical and Analytical Chemistry

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 532 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf