Crystallization and preliminary X-ray analysis of heparinase II from Pedobacter heparinus

Download
  1. Get@NRC: Crystallization and preliminary X-ray analysis of heparinase II from Pedobacter heparinus (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1107/S0907444904016695
AuthorSearch for: ; Search for: ; Search for:
TypeArticle
Journal titleActa Crystallographica Section D
Volume60
IssuePt 9
Pages16441646; # of pages: 3
Subjectanalysis; Crystallization; Enzymes; Molecular Weight; pha; x-ray
AbstractHeparinase II from Pedobacter heparinus (formerly Flavobacterium heparinum), which acts on both heparin and heparan sulfate, is one of several glycosaminoglycan-degrading enzymes produced by this organism. This enzyme, with a molecular weight of 84 kDa, utilizes a lytic mechanism to cleave the alpha(1-4) glycosidic bond between hexosamine (D-glucosamine) and L-iduronic or D-glucuronic acid, resulting in a product with an unsaturated sugar ring at the non-reducing end. The enzyme was crystallized by the hanging-drop vapour -diffusion method. The crystals belong to orthorhombic space group P2(1)2(1)2(1) and diffract to 2 A resolution. There are two molecules in the asymmetric unit, consistent with the finding that recombinant heparinase II functions as a dimer in solution
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
NoteEnglish15333943
Peer reviewedNo
NRC number46220
NPARC number3539273
Export citationExport as RIS
Report a correctionReport a correction
Record identifier027c7fad-b9fa-42b1-ac88-b3750ae99e2c
Record created2009-03-01
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)