4pvq

Revision as of 12:15, 26 March 2014 by OCA (talk | contribs) (Protected "4pvq" [edit=sysop:move=sysop])

Template:STRUCTURE 4pvq

Crystal structure of sulfate-bound human l-asparaginase proteinCrystal structure of sulfate-bound human l-asparaginase protein

Template:ABSTRACT PUBMED 22861376

FunctionFunction

[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 StructureAbout this Structure

4pvq is a 2 chain structure. This structure supersedes the now removed PDB entry 4gdu. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. 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
  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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