CHEBI:85924 - (1S,2S)-1,2-dihydroxypropylphosphonic acid

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ChEBI Name (1S,2S)-1,2-dihydroxypropylphosphonic acid ChEBI ID CHEBI:85924 ChEBI ASCII Name (1S,2S)-1,2-dihydroxypropylphosphonic acid Definition A member of the class of phosphonic acids that is propylphosphonic acid substituted by hydroxy groups at positions 1 and 2 (the 1S,2S-stereoisomer). Stars This entity has been manually annotated by the ChEBI Team. Supplier Information No supplier information found for this compound. Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C3H9O5P Net Charge 0 Average Mass 156.07430 Monoisotopic Mass 156.01876 InChI InChI=1S/C3H9O5P/c1-2(4)3(5)9(6,7)8/h2-5H,1H3,(H2,6,7,8)/t2-,3-/m0/s1 InChIKey MXMXXUIOCREOTJ-HRFVKAFMSA-N SMILES C[C@H](O)[C@@H](O)P(O)(O)=O ChEBI Ontology Outgoing (1S,2S)-1,2-dihydroxypropylphosphonic acid (CHEBI:85924) is a glycol (CHEBI:13643) (1S,2S)-1,2-dihydroxypropylphosphonic acid (CHEBI:85924) is a phosphonic acids (CHEBI:26069) (1S,2S)-1,2-dihydroxypropylphosphonic acid (CHEBI:85924) is a secondary alcohol (CHEBI:35681) (1S,2S)-1,2-dihydroxypropylphosphonic acid (CHEBI:85924) is conjugate acid of (1S,2S)-1,2-dihydroxypropylphosphonate(1−) (CHEBI:85581) Incoming (1S,2S)-1,2-dihydroxypropylphosphonate(1−) (CHEBI:85581) is conjugate base of (1S,2S)-1,2-dihydroxypropylphosphonic acid (CHEBI:85924) IUPAC Name [(1S,2S)-1,2-dihydroxypropyl]phosphonic acid Registry Number Type Source 7578761 Reaxys Registry Number Reaxys Citation Fillgrove KL, Pakhomova S, Newcomer ME, Armstrong RN (2003) Mechanistic diversity of fosfomycin resistance in pathogenic microorganisms. Journal of the American Chemical Society 125, 15730-15731 [PubMed:14677948] [show Abstract] Microbial resistance to the antibiotic fosfomycin [(1R,2S)-epoxypropylphosphonic acid, 1] is known to be mediated by thiol transferase enzymes FosA and FosB, which catalyze the addition of glutathione and l-cysteine to C1 of the oxirane, respectively. A probe of the microbial genome database reveals a related group of enzymes (FosX). The genes mlr3345 from Mesorhizobium loti and lmo1702 from Listeria monocytogenes were cloned and the proteins expressed. This heretofore unrecognized group of enzymes is shown to catalyze the Mn(II)-dependent addition of water to C1 of the oxirane. The ability of each enzyme to confer resistance in Escherichia coli is correlated with their catalytic efficiency, such that the M. loti protein confers low resistance while the Listeria enzyme confers very robust resistance. The crystal structure of the FosX from M. loti was solved at a resolution of 1.83 A. The structure reveals an active-site carboxylate (E44) located about 5 A from the expected position of the substrate that appears to be poised to participate in catalysis. Single turnover experiments in H218O and kinetic analysis of the E44G mutant of the FosX enzymes indicate that the carboxylate of E44 acts as a general base in the direct addition of water to 1. The FosX from M. loti also catalyzes the addition of glutathione to the antibiotic. The catalytic promiscuity and low efficiency of the M. loti protein suggest that it may be an intermediate in the evolution of clinically relevant fosfomycin resistance proteins such as the FosX from Listeria monocytogenese. Last Modified 03 June 2015