4osy: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4osy|  PDB=4osy  |  SCENE=  }}
===STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN===
{{ABSTRACT_PUBMED_23601642}}


The entry 4osy is ON HOLD
==Function==
[[http://www.uniprot.org/uniprot/ASGL1_HUMAN 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.<ref>PMID:19839645</ref> 


Authors: Nomme, J, Lavie, A
==About this Structure==
[[4osy]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4hlp 4hlp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OSY OCA].


Description: STRUCTURE OF FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN
==Reference==
<ref group="xtra">PMID:023601642</ref><references group="xtra"/><references/>
[[Category: Lavie, A.]]
[[Category: Nomme, J.]]
[[Category: Hydrolase]]
[[Category: Ntn enzyme]]

Revision as of 13:27, 12 March 2014

Template:STRUCTURE 4osy

STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN

Template:ABSTRACT PUBMED 23601642

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

  1. 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
  1. ↑ 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

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