0-Hydroxypropionate dehydrogenase

Den el al. (108) purified a DPN-dependent jS-hydroxypropionate dehydrogenase 200-fold from pig kidney which catalyzes the reaction of... 

Lactic acid (2-hydroxypropionic acid) is perhaps the most widely occurring carboxylic acid in nature. The Swedish chemist Scheele first discovered it in 1780. It exists in two different forms (Fig. 1) the dextrorotatory form, called L(-i-)-lactic acid or (5)-lactic acid, and the levorotatory form, called D(-)-lactic acid or R)-lactic acid. The plus and minus signs indicate the direction of the rotation of plane-polarized light produced by a chemical. These 2 stereoisomers (scientifically known as enantiomers ) are produced by different enzymes [lactate dehydrogenases (LDH)] present in living organisms. In this chapter, they will be referred to as D-lactic acid (d-LA) and L-lactic acid (l-LA). Naturally formed lactic acid is usually in the l form, but d-LA may coexist with l-LA in some cases, especially if it is secreted by nonspecific microbes. 

Kumar V, Sankaranarayanan M, Jae KE, Durgapal M, Ashok S, Ko Y, Sarkar R, Park S. (2012). Co-production of 3-hydroxypropionic acid and 1,3-propanediol from glycerol using resting cells of recombinant Klebsiella pneumoniae J2B strain overexpressing aldehyde dehydrogenase. Appl Microbiol Biotechnol, 96,373-383. 

Ko Y, Ashok S, Zhou S, Kumar V, Park S. (2012) Aldehyde dehydrogenase activity is important to the production of 3-hydroxypropionic acid from glycerol by recombinant Klebsiella pneumoniae. Process Biochem, 47, 1135-1143. 

Luo LH, Kim CH, Heo SY, Oh BR, Hong WK, Kim S, Kim DH, Seo JW. (2012). Produe-tion of 3-hydroxypropionic acid through propionaldehyde dehydrogenase PduP mediated biosynthetic pathway in Klebsiella pneumoniae. Bioresour Technol, 103,1-6. 

Examination of plasma and urine revealed elevated quantities of jff-ala-nine, 3-hydroxypropionic acid, (R)- and (S)-3-aminoisobutyric acid, (R)-and (S)-3-hydroxyisobutyric acid and (S)-2-hydroxymethylbutyric acid. Direct enzymatic assay of methylmalonate semialdehyde dehydrogenase is unavailable revealed homozygosity for DNA analysis 1336 G>A transversion which substituted an arginine for a highly conserved glycine at amino acid residue 446. 

Figure 14 Production of 3-hydroxypropionic add as a nrtetabolic intermediate and an end product via 3-hydroxypropionate pathway in ChlCH ofiexus aurantiacus. Enzymes accACD, acetyl-CoA carboxylase mcr, malonyl-CoA reductase pcs, propionyl-CoA synthase pcc, propionyl-CoA carboxylase mcee, methylmalonyl-CoA epimerase mut, methylmalonyl-CoA mutase smtAB, sucdnyl-CoA (S)-malate-CoA transferase sdh, succinate dehydrogenase fh, fumarate hydratase mcl, (S)-malyl-CoA/-methylmalyl-CoA/(S)-citramalyl-CoA (MMC) lyase mch, methylmalyl-CoA dehydratase met, mesaconyl-CoA-Cl-C4 CoA transferase and meh, mesaconyl-C4-CoA hydratase [10] (Reference Metacyc).

Hydroxypropionaldehyde-specific aldehyde dehydrogenase from Bacillus subtilis catalyzes 3-hydroxypropionic acid production in Klebsiella pneumoniae. Biotechnd. Lett, 37 (3), 717-724. 

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