Glycosylasparaginase
From Proteopedia
(Difference between revisions)
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**[[1ayy]], [[2gaw]] – EmAGA α+β subunits – ''Elizabethkingia meningoseptica''<br /> | **[[1ayy]], [[2gaw]] – EmAGA α+β subunits – ''Elizabethkingia meningoseptica''<br /> | ||
| - | **[[5v2i]] – EmAGA α+β (mutant) subunits <br /> | + | **[[5v2i]], [[6dey]] – EmAGA α+β (mutant) subunits <br /> |
**[[1apy]] – hAGA + Nag + β-mannose - human<br /> | **[[1apy]] – hAGA + Nag + β-mannose - human<br /> | ||
**[[1apz]] – hAGA + Nag + β-mannose + Asp<br /> | **[[1apz]] – hAGA + Nag + β-mannose + Asp<br /> | ||
Revision as of 06:12, 16 July 2019
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3D structures of glycosylasparaginase
Updated on 16-July-2019
References
- ↑ Qian X, Guan C, Guo HC. A dual role for an aspartic acid in glycosylasparaginase autoproteolysis. Structure. 2003 Aug;11(8):997-1003. PMID:12906830
- ↑ Ikonen E, Peltonen L. Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease. Hum Mutat. 1992;1(5):361-5. PMID:1301945 doi:http://dx.doi.org/10.1002/humu.1380010503
- ↑ Wang Y, Guo HC. Crystallographic snapshot of a productive glycosylasparaginase-substrate complex. J Mol Biol. 2007 Feb 9;366(1):82-92. Epub 2006 Sep 26. PMID:17157318 doi:10.1016/j.jmb.2006.09.051
