Glycosylasparaginase
From Proteopedia
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| - | <StructureSection load='2gl9' size='340' side='right' caption='Structure of glycosylated human glycosylasparaginase α ( | + | <StructureSection load='2gl9' size='340' side='right' caption='Structure of glycosylated human glycosylasparaginase α (magenta and cyan) and β (green and yellow) subunits complex with asparagine (PDB code [[2gl9]]).' scene='59/591999/Cv/1'> |
== 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. | + | AGA deficiency is the cause of the human lysosomal disease aspartylglycosaminuria<ref>PMID:1301945</ref>. |
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== Structural highlights == | == Structural highlights == | ||
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| + | <scene name='59/591999/Cv/6'>Glycosylated human glycosylasparaginase α and β subunits with asparagine</scene>. Mammalian <scene name='59/591999/Cv/7'>AGA substrate is the protein-sugar bond of Asn-GlcNag</scene><ref>PMID:17157318</ref>. Water molecules shown as red spheres. | ||
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| + | == See also [[Asparaginase]] == | ||
</StructureSection> | </StructureSection> | ||
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*AGA α+β subunits | *AGA α+β subunits | ||
| - | **[[1ayy]], [[2gaw]] – EmAGA α+β subunits – ''Elizabethkingia meningoseptica''<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 /> | ||
| + | **[[1ayy]], [[2gaw]] – EmAGA α+β subunits – ''Elizabethkingia meningoseptica''<br /> | ||
| + | **[[5v2i]], [[6dey]] – EmAGA α+β (mutant) subunits <br /> | ||
**[[2gl9]] – EmAGA α+β (mutant) subunits + Nag + Asn<br /> | **[[2gl9]] – EmAGA α+β (mutant) subunits + Nag + Asn<br /> | ||
| + | **[[4r4y]] – EmAGA α+β (mutant) subunits + hydroxyl-Asn<br /> | ||
| + | **[[1pgs]] – EmAGA α+β subunits – ''Flavobacterium meningoseptica''<br /> | ||
*AGA precursor | *AGA precursor | ||
Current revision
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3D structures of glycosylasparaginase
Updated on 09-April-2023
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
