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Asparaginase

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== Function ==
== Function ==
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'''Asparaginase''' (ASP) catalyzes the conversion of asparagine to aspartic acid (AA). The ALL cells require high concentrations of asparagine which becomes scarce when high doses of ASP are present. '''Isoaspartyl peptidase/L-asparaginase''' (IPA) has activity of L-asparaginase and of β-aspartyl peptidase<ref>PMID:15159592</ref>.
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'''Asparaginase''' (ASP) catalyzes the conversion of asparagine to aspartic acid (AA). The ALL cells require high concentrations of asparagine which becomes scarce when high doses of ASP are present. '''Isoaspartyl peptidase/L-asparaginase''' (IPA) has activity of L-asparaginase and of β-aspartyl peptidase<ref>PMID:15159592</ref>. '''Glycosylasparaginase''' (GASP) plays an imortant role in asparagine-linked glycoprotein degradation<ref>PMID:17157318</ref>.
== Relevance ==
== Relevance ==
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ASP I is used in the food processing industry to reduce the formation of the carcinogen acrylamide in the production of starchy food products<ref>PMID:27211635</ref>. A different kind of ASP – ASP II – is used as drug (Elspar) in the treatment of cancer such as acute lymphoblastic leukemia (ALL)<ref>PMID:15651203</ref>.
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ASP I is used in the food processing industry to reduce the formation of the carcinogen acrylamide in the production of starchy food products<ref>PMID:27211635</ref>. A different kind of ASP – ASP II – is used as drug (Elspar) in the treatment of cancer such as acute lymphoblastic leukemia (ALL)<ref>PMID:15651203</ref>.
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== Disease ==
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GASP mutants cause the autosomal recessive lysosomal storage disease aspartylglycosaminuria<ref>PMID:10571008</ref>.
== Structural highlights ==
== Structural highlights ==
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*<scene name='52/525144/Cv/7'>Aspartic acid binding site</scene>, chain A.
*<scene name='52/525144/Cv/7'>Aspartic acid binding site</scene>, chain A.
*<scene name='52/525144/Cv/8'>Cl coordination site</scene>.
*<scene name='52/525144/Cv/8'>Cl coordination site</scene>.
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==3D structures of asparaginase==
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[[Asparaginase 3D structures]]
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</StructureSection>
</StructureSection>
==3D structures of asparaginase==
==3D structures of asparaginase==
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**[[1wsa]] – WsASP precursor <br />
**[[1wsa]] – WsASP precursor <br />
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**[[6eok]] - EcASP (mutant)<br />
**[[1ihd]], [[1jaz]], [[1jja]], [[5mq5]] - EcASP (mutant)
**[[1ihd]], [[1jaz]], [[1jja]], [[5mq5]] - EcASP (mutant)
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**[[4o0h]] - hIPA + L-Asp<br />
**[[4o0h]] - hIPA + L-Asp<br />
**[[4osx]], [[4osy]] - hIPA + Gly<br />
**[[4osx]], [[4osy]] - hIPA + Gly<br />
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*Glycosylasparaginase or N(4)-(b-N-acetylglucosaminyl)-L-asparaginase
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**[[9gaa]] - EmGASP – Elizabethkingia meningoseptica<br />
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**[[9gac]], [[9gaf]], [[5v2i]], [[3ljq]] - EmGASP (mutant) <br />
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**[[2gl9]], [[4r4y]] - EmGASP (mutant) + Asn<br />
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*Glutaminase-asparaginase see [[Glutaminase]]
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**[[2zak]], [[3c17]] - EcASP precursor (mutant)
**[[2zak]], [[3c17]] - EcASP precursor (mutant)
}}
}}

Revision as of 09:15, 20 March 2019

E. coli asparaginase I tetramer complex with aspartic acid, asparagine, ethylene glycol and Cl- ions (green), 2p2n

Drag the structure with the mouse to rotate

3D structures of asparaginase

Updated on 20-March-2019

References

  1. ↑ Prahl A, Pazgier M, Hejazi M, Lockau W, Lubkowski J. Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1173-6. Epub 2004, May 21. PMID:15159592 doi:10.1107/S0907444904003403
  2. ↑ 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
  3. ↑ Xu F, Oruna-Concha MJ, Elmore JS. The use of asparaginase to reduce acrylamide levels in cooked food. Food Chem. 2016 Nov 1;210:163-71. doi: 10.1016/j.foodchem.2016.04.105. Epub 2016 , Apr 22. PMID:27211635 doi:http://dx.doi.org/10.1016/j.foodchem.2016.04.105
  4. ↑ Kwok CS, Kham SK, Ariffin H, Lin HP, Quah TC, Yeoh AE. Escherichia coli-asparaginase (Elspar) is superior to Erwinia-asparaginase (Erwinase) in childhood acute lymphoblastic leukaemia (ALL) induction--an early response study using minimal residual disease (MRD) markers. Ann Acad Med Singapore. 2004 Sep;33(5 Suppl):S45-6. PMID:15651203
  5. ↑ Aronson NN Jr. Aspartylglycosaminuria: biochemistry and molecular biology. Biochim Biophys Acta. 1999 Oct 8;1455(2-3):139-54. PMID:10571008
  6. ↑ Yun MK, Nourse A, White SW, Rock CO, Heath RJ. Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I. J Mol Biol. 2007 Jun 8;369(3):794-811. Epub 2007 Mar 30. PMID:17451745 doi:http://dx.doi.org/10.1016/j.jmb.2007.03.061

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