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Asparaginase
From Proteopedia
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== Function == | == Function == | ||
| - | ''' | + | '''L-Asparaginases''' are enzymes that hydrolyze the amide group of the amino acid L-asparagine (L-Asn) to L-aspartate, with the simultaneous release of ammonia. They are often referred to as ASNase and assigned the EC number 3.5.1.1; if significant glutaminase co-activity (hydrolysis of the similar amino acid L-glutamine) is also present, the EC number is 3.5.1.38. Some ASNases that belong to other classes (see below) are assigned EC 3.4.19.5. (GASP) plays an imortant role in asparagine-linked glycoprotein degradation<ref>PMID:17157318</ref>. |
== Relevance == | == Relevance == | ||
Revision as of 07:15, 29 April 2024
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References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Aronson NN Jr. Aspartylglycosaminuria: biochemistry and molecular biology. Biochim Biophys Acta. 1999 Oct 8;1455(2-3):139-54. PMID:10571008
- ↑ 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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