constitutively synthesized, no regulatory function in the methylcitric acid cycle. The enzyme is supposed to have evolutionarily developed from a hypothetical and prototypical isocitrate dehydratase
constitutively synthesized, no regulatory function in the methylcitric acid cycle. The enzyme is supposed to have evolutionarily developed from a hypothetical and prototypical isocitrate dehydratase
the absence of 2-methylisocitrate dehydratase, PrpD, is compensated by the activity of SoAcnD and SoPrpF, SoAcnD has 2-methylcitrate dehydratase (EC 4.2.1.79) activity and PrpF has aconitate isomerase (EC 5.3.3.7) activity
transposon mutagenesis. In one disulfide 3,3â-dithiodipropionic acid (DTDP)-negative (Jhw13b) and one DTDP-leaky (JhwAA14) mutant, Tn5::mob is mapped in a gene encoding a putative bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase (AcnB, EC 4.2.1.3). AcnB dehydrates 2-methylcitric acid to 2-methyl-cis-aconitic acid and subsequently hydrates it to 2-methylisocitric acid
transposon mutagenesis. In one disulfide 3,3â-dithiodipropionic acid (DTDP)-negative (Jhw13b) and one DTDP-leaky (JhwAA14) mutant, Tn5::mob is mapped in a gene encoding a putative bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase (AcnB, EC 4.2.1.3). AcnB dehydrates 2-methylcitric acid to 2-methyl-cis-aconitic acid and subsequently hydrates it to 2-methylisocitric acid
transposon mutagenesis. In one disulfide 3,3â-dithiodipropionic acid (DTDP)-negative (Jhw13b) and one DTDP-leaky (JhwAA14) mutant, Tn5::mob is mapped in a gene encoding a putative bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase (AcnB, EC 4.2.1.3). AcnB dehydrates 2-methylcitric acid to 2-methyl-cis-aconitic acid and subsequently hydrates it to 2-methylisocitric acid
Wuebbeler, J.H.; Bruland, N.; Kretschmer, K.; Steinbuechel, A.
Novel pathway for catabolism of the organic sulfur compound 3,3-dithiodipropionic acid via 3-mercaptopropionic acid and 3-Sulfinopropionic acid to propionyl-coenzyme A by the aerobic bacterium Tetrathiobacter mimigardefordensis strain DPN7
The PrpF protein of Shewanella oneidensis MR-1 catalyzes the isomerization of 2-methyl-cis-aconitate during the catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle