4osy | pdb_00004osy
From Proteopedia
STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN
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
4osy is a 2 chain structure. This structure supersedes the now removed PDB entry 4hlp. Full crystallographic information is available from OCA.
Reference
- Su Y, Karamitros CS, Nomme J, McSorley T, Konrad M, Lavie A. Free glycine accelerates the autoproteolytic activation of human asparaginase. Chem Biol. 2013 Apr 18;20(4):533-40. doi: 10.1016/j.chembiol.2013.03.006. PMID:23601642 doi:https://dx.doi.org/10.1016/j.chembiol.2013.03.006
- ↑ 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
