4ast
The apo structure of a bacterial aldo-keto reductase AKR14A1The apo structure of a bacterial aldo-keto reductase AKR14A1
Template:ABSTRACT PUBMED 23103600
FunctionFunction
[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 StructureAbout this Structure
4ast is a 8 chain structure with sequence from Ecobd. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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