Glycosylasparaginase

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(New page: <StructureSection load='2gl9' size='340' side='right' caption='Structure of glycosylated human glycosylasparaginase α and β subunits complex with asparagine (PDB code 2gl9).' scene=...)
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<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'>
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<StructureSection load='2gl9' size='340' side='right' caption='Structure of glycosylated human glycosylasparaginase α and β subunits complex with asparagine (PDB code [[2gl9]]).' scene=''>
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== Function ==
== Function ==
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'''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. Mammalian AGA substrate is the protein-sugar bond of Asn-GlcNac.
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'''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 ==
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AGA deficiency is the cause of the human lysosomal disease aspartylglycosaminuria.
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AGA deficiency is the cause of the human lysosomal disease aspartylglycosaminuria<ref>PMID:1301945</ref>.
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== Relevance ==
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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]] ==
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</StructureSection>
==3D structures of glycosylasparaginase==
==3D structures of glycosylasparaginase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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'''AGA α+β subunits'''
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*AGA α+β subunits
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[[1ayy]], [[2gaw]] – EmAGA α+β subunits – ''Elizabethkingia meningoseptica''<br />
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[[1apy]] – hAGA + Nag + β-mannose - human<br />
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[[1apz]] – hAGA + Nag + β-mannose + Asp<br />
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[[2gl9]] – EmAGA α+β (mutant) subunits + Nag + Asn<br /
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'''AGA precursor'''
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**[[1apy]] – hAGA + Nag + β-mannose - human<br />
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**[[1apz]] – hAGA + Nag + β-mannose + Asp<br />
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**[[1ayy]], [[2gaw]] – EmAGA α+β subunits – ''Elizabethkingia meningoseptica''<br />
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**[[5v2i]], [[6dey]] – EmAGA α+β (mutant) subunits <br />
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**[[2gl9]] – EmAGA α+β (mutant) subunits + Nag + Asn<br />
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**[[4r4y]] – EmAGA α+β (mutant) subunits + hydroxyl-Asn<br />
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**[[1pgs]] – EmAGA α+β subunits – ''Flavobacterium meningoseptica''<br />
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[[2gac]] - EmPAGA (mutant)<br />
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*AGA precursor
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[[9gaa]], [[1p4k]] – EmPAGA (mutant)<br />
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[[9gac]], [[9gaf]], [[1p4v]], [[3ljq]] – EmPAGA (mutant) + glycine<br />
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**[[2gac]] - EmPAGA (mutant)<br />
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**[[9gaa]], [[1p4k]] – EmPAGA (mutant)<br />
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**[[9gac]], [[9gaf]], [[1p4v]], [[3ljq]] – EmPAGA (mutant) + glycine<br />
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}}
== References ==
== References ==

Current revision

Structure of glycosylated human glycosylasparaginase α (magenta and cyan) and β (green and yellow) subunits complex with asparagine (PDB code 2gl9).

Drag the structure with the mouse to rotate

3D structures of glycosylasparaginase

Updated on 09-April-2023

References

  1. 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
  2. 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
  3. 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

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Michal Harel, Alexander Berchansky

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