Glycosylasparaginase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Glycosylasparaginase''' or '''aspartylglucosaminidase''' (AGA) hydrolyzes a number of β-aspartyl amides including asparagine. AGA contains α and β subunits which derive from a precursor (PAGA) which is cleaved post-translationally | + | '''Glycosylasparaginase''' or '''aspartylglucosaminidase''' (AGA) hydrolyzes a number of β-aspartyl amides including asparagine. AGA contains α and β subunits which derive from a precursor (PAGA) which is cleaved post-translationally<ref>PMID:12906830</ref>. |
== Disease == | == Disease == | ||
AGA deficiency is the cause of the human lysosomal disease aspartylglycosaminuria<ref>PMID:1301945</ref>. | AGA deficiency is the cause of the human lysosomal disease aspartylglycosaminuria<ref>PMID:1301945</ref>. | ||
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| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
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| + | Mammalian AGA substrate is the protein-sugar bond of Asn-GlcNac<ref>PMID:17157318</ref>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:34, 14 March 2016
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3D structures of glycosylasparaginase
Updated on 14-March-2016
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
