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4osy

From Proteopedia

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m (Protected "4osy" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4osy| PDB=4osy | SCENE= }}
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===STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN===
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{{ABSTRACT_PUBMED_23601642}}
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The entry 4osy is ON HOLD
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==Function==
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[[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>
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Authors: Nomme, J, Lavie, A
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==About this Structure==
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[[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].
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Description: STRUCTURE OF FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN
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==Reference==
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<ref group="xtra">PMID:023601642</ref><references group="xtra"/><references/>
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[[Category: Lavie, A.]]
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[[Category: Nomme, J.]]
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[[Category: Hydrolase]]
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[[Category: Ntn enzyme]]

Revision as of 13:27, 12 March 2014

Template:STRUCTURE 4osy

Contents

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

  • 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:http://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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