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4aub

From Proteopedia

Revision as of 13:36, 12 March 2014 by OCA (Talk | contribs)
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Template:STRUCTURE 4aub

Contents

the complex Structure of the bacterial aldo-keto reductase AKR14A1 with NADP and citrate

Template:ABSTRACT PUBMED 23103600

Function

[GPR_ECOLI] Catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). The physiological role of gpr is the detoxification of L-GAP, which may be formed by non-enzymatic racemization of GAP. Also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.[1] [2] [3]

About this Structure

4aub is a 8 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA.

Reference

  • Lapthorn AJ, Zhu X, Ellis EM. The diversity of microbial aldo/keto reductases from Escherichia coli K12. Chem Biol Interact. 2013 Feb 25;202(1-3):168-77. doi: 10.1016/j.cbi.2012.10.008. , Epub 2012 Oct 24. PMID:23103600 doi:http://dx.doi.org/10.1016/j.cbi.2012.10.008
  1. Grant AW, Steel G, Waugh H, Ellis EM. A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity. FEMS Microbiol Lett. 2003 Jan 21;218(1):93-9. PMID:12583903
  2. Ko J, Kim I, Yoo S, Min B, Kim K, Park C. Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases. J Bacteriol. 2005 Aug;187(16):5782-9. PMID:16077126 doi:http://dx.doi.org/10.1128/JB.187.16.5782-5789.2005
  3. Desai KK, Miller BG. A metabolic bypass of the triosephosphate isomerase reaction. Biochemistry. 2008 Aug 5;47(31):7983-5. doi: 10.1021/bi801054v. Epub 2008 Jul 12. PMID:18620424 doi:http://dx.doi.org/10.1021/bi801054v

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