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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>. '''Glycosylasparaginase''' (GASP) plays an imortant role in asparagine-linked glycoprotein degradation<ref>PMID:17157318</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 ==

Revision as of 12:12, 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

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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