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4osx
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4osx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4hlo 4hlo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OSX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OSX FirstGlance]. <br> | <table><tr><td colspan='2'>[[4osx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4hlo 4hlo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OSX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OSX FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4osy|4osy]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4osy|4osy]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALP, ASRGL1, CRASH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALP, ASRGL1, CRASH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4osx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4osx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4osx RCSB], [http://www.ebi.ac.uk/pdbsum/4osx PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4osx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4osx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4osx RCSB], [http://www.ebi.ac.uk/pdbsum/4osx PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Free glycine accelerates the autoproteolytic activation of human asparaginase.,Su Y, Karamitros CS, Nomme J, McSorley T, Konrad M, Lavie A Chem Biol. 2013 Apr 18;20(4):533-40. doi: 10.1016/j.chembiol.2013.03.006. PMID:23601642<ref>PMID:23601642</ref> | Free glycine accelerates the autoproteolytic activation of human asparaginase.,Su Y, Karamitros CS, Nomme J, McSorley T, Konrad M, Lavie A Chem Biol. 2013 Apr 18;20(4):533-40. doi: 10.1016/j.chembiol.2013.03.006. PMID:23601642<ref>PMID:23601642</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| - | [[Category: Lavie, A | + | [[Category: Lavie, A]] |
| - | [[Category: Nomme, J | + | [[Category: Nomme, J]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Ntn enzyme]] | [[Category: Ntn enzyme]] | ||
Revision as of 03:58, 25 December 2014
STRUCTURE of UNCLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN
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Categories: Human | Lavie, A | Nomme, J | Hydrolase | Ntn enzyme
