Abstract:
:A detailed knowledge about the substrate specificities of the heparin lyases is necessary when using these enzymes as tools for elucidating the sequence of heparin and heparan sulfate. The substrate specificity of heparin lyases I, II, and III have been profiled with structurally defined, heparin-derived oligosaccharides. The primary substrate specificities of heparin lyases I and III require the presence of 2-O-sulfated alpha-L-idopyranosyluronic acid and beta-D-glucopyranosyluronic acid residues, respectively, at the linkages being cleaved. Heparin lyase II demonstrates an intriguingly broad primary specificity for oligosaccharides, acting at linkages containing alpha-L-idopyranosyluronic and beta-D-glucopyranosyluronic acid as well as at linkages containing alpha-L-galactopyranosyluronic acid residues. In addition to their primary specificities, each lyase also demonstrates secondary specificities under forcing conditions. Differences in the sulfation pattern within uronic acid residues and sulfation of adjacent residues has profound impact on the ease of lyase cleavage of a glycosidic linkage. Specifically, heparin lyases I and III exhibit secondary specificity for oligosaccharides containing an unsulfated alpha-L-idopyranosyluronic acid residue. The lack of sulfation on residues adjacent to the linkage undergoing cleavage increases the action of heparin lyase III on a glycosidic linkage. In contrast, reduced sulfation on adjacent residues make glycosidic linkage resistant to heparin lyase I. The primary and secondary specificity can be rationalized on the basis of most favorable solution conformation of the uronic acid residues.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Desai UR,Wang HM,Linhardt RJdoi
10.1006/abbi.1993.1538subject
Has Abstractpub_date
1993-11-01 00:00:00pages
461-8issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(83)71538-9journal_volume
306pub_type
杂志文章abstract::The present paper focussed on the mechanistic aspect of the reaction of singlet oxygen (1O2), in its lowest excited state (1 Delta g), toward DNA constituents. It is well known that 1O2 is able to react with the guanine moiety of DNA to produce almost specifically 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodGuo). Howev...
journal_title:Archives of biochemistry and biophysics
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pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:2010-12-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1993.1496
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:2004-12-15 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1016/j.abb.2007.10.010
更新日期:2008-01-15 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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更新日期:1993-03-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章,评审
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abstract::Four subunits of beta-conglycinin were purified from soybean cultivar CX 635-1-1-1, and were designated alpha, alpha', beta, and beta' in accordance with nomenclature proposed by Thanh and Shibasaki [(1977) Biochim. Biophys. Acta 490, 370-384]. Of these subunits, beta' has not previously been reported or characterized...
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pub_type: 杂志文章,评审
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1985-07-01 00:00:00