View : 25 Download: 0

Crystallization and preliminary X-ray analysis of neoagarobiose hydrolase from Saccharophagus degradans 2-40

Title
Crystallization and preliminary X-ray analysis of neoagarobiose hydrolase from Saccharophagus degradans 2-40
Authors
Lee S.Lee J.Y.Ha S.C.Jung J.Shin D.H.Kim K.H.Choi I.-G.
Ewha Authors
신동해
SCOPUS Author ID
신동해scopus
Issue Date
2009
Journal Title
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
ISSN
1744-3091JCR Link
Citation
vol. 65, no. 12, pp. 1299 - 1301
Indexed
SCOPUS WOS scopus
Abstract
Many agarolytic bacteria degrade agar polysaccharide into the disaccharide unit neoagarobiose [O-3,6-anhydro -α L-galactopyranosyl-(1→3)-D- galactose] using various β-agarases. Neoagarobiose hydrolase is an enzyme that acts on the α- 1,3 linkage in neoagarobiose to yield D-galactose and 3,6-anhydro-L-galactose. This activity is essential in both the metabolism of agar by agarolytic bacteria and the production of fermentable sugars from agar biomass for bioenergy production. Neoagarobiose hydrolase from the marine bacterium Saccharophagus degradans 2-40 was overexpressed in Escherichia coli and crystallized in the monoclinic space group C2, with unit-cell parameters a = 129.83, b = 76.81, c = 90.11 Å, β = 101.86°. The crystals diffracted to 1.98 Å resolution and possibly contains two molecules in the asymmetric unit. © 2009 International Union of Crystallography All rights reserved.
DOI
10.1107/S174430910904603X
Appears in Collections:
약학대학 > 약학과 > Journal papers
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE