We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Asparaginase
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Function == | == Function == | ||
| - | '''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. | + | '''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>. |
== Relevance == | == Relevance == | ||
Revision as of 10:14, 22 March 2018
| |||||||||||
3D structures of asparaginase
Updated on 22-March-2018
References
- ↑ 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
- ↑ 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
Proteopedia Page Contributors and Editors (what is this?)
Joel L. Sussman, Michal Harel, Alexander Berchansky, Jaime Prilusky
