This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4pvp
From Proteopedia
Contents |
Crystal structure of malonate-bound human L-asparaginase protein
Template:ABSTRACT PUBMED 22861376
Function
[ASGL1_HUMAN] Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.[1]
About this Structure
4pvp is a 2 chain structure. This structure supersedes the now removed PDB entry 4gdt. Full crystallographic information is available from OCA.
Reference
- Nomme J, Su Y, Konrad M, Lavie A. Structures of Apo and Product-Bound Human l-Asparaginase: Insights into the Mechanism of Autoproteolysis and Substrate Hydrolysis. Biochemistry. 2012 Aug 28;51(34):6816-26. Epub 2012 Aug 14. PMID:22861376 doi:http://dx.doi.org/10.1021/bi300870g
- ↑ Cantor JR, Stone EM, Chantranupong L, Georgiou G. The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity. Biochemistry. 2009 Nov 24;48(46):11026-31. doi: 10.1021/bi901397h. PMID:19839645 doi:10.1021/bi901397h
Categories: Lavie, A. | Nomme, J. | Homodimer | Hydrolase | L-asparagine | Ntn enzyme
