4mmh
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_4mmh| PDB=4mmh | SCENE= }} | {{STRUCTURE_4mmh| PDB=4mmh | SCENE= }} | ||
===Crystal structure of heparan sulfate lyase HepC from Pedobacter heparinus=== | ===Crystal structure of heparan sulfate lyase HepC from Pedobacter heparinus=== | ||
| + | {{ABSTRACT_PUBMED_24437462}} | ||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
| - | <references group="xtra"/><references/> | + | <ref group="xtra">PMID:024437462</ref><references group="xtra"/><references/> |
[[Category: Heparin-sulfate lyase]] | [[Category: Heparin-sulfate lyase]] | ||
[[Category: Hashimoto, W.]] | [[Category: Hashimoto, W.]] | ||
Revision as of 09:16, 5 February 2014
Contents |
Crystal structure of heparan sulfate lyase HepC from Pedobacter heparinus
Template:ABSTRACT PUBMED 24437462
Function
[HEPC_PEDHD] Specifically cleaves heparan sulfate-rich regions of acidic polysaccharides. Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages. Functions in cleaving metazoan heparan sulfate and providing carbon, nitrogen and sulfate sources for microorganisms.[1] [2]
About this Structure
4mmh is a 1 chain structure. Full crystallographic information is available from OCA.
Reference
- Hashimoto W, Maruyama Y, Nakamichi Y, Mikami B, Murata K. Crystal Structure of Pedobacter heparinus Heparin Lyase Hep III with the Active Site in a Deep Cleft. Biochemistry. 2014 Feb 4;53(4):777-86. doi: 10.1021/bi4012463. Epub 2014 Jan 27. PMID:24437462 doi:http://dx.doi.org/10.1021/bi4012463
- ↑ Su H, Blain F, Musil RA, Zimmermann JJ, Gu K, Bennett DC. Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum. Appl Environ Microbiol. 1996 Aug;62(8):2723-34. PMID:8702264
- ↑ Pojasek K, Shriver Z, Hu Y, Sasisekharan R. Histidine 295 and histidine 510 are crucial for the enzymatic degradation of heparan sulfate by heparinase III. Biochemistry. 2000 Apr 11;39(14):4012-9. PMID:10747789
