Microbial growth on oxalate by a route not involving glyoxylate carboligase

Abstract

1. The metabolism of oxalate by the pink-pigmented organisms, Pseudomonas AM1, Pseudomonas AM2, Protaminobacter ruber and Pseudomonas extorquens has been compared with that of the non-pigmented Pseudomonas oxalaticus. 2. During growth on oxalate, all the organisms contain oxalyl-CoA decarboxylase, formate dehydrogenase and oxalyl-CoA reductase. This is consistent with oxidation of oxalate to carbon dioxide taking place via oxalyl-CoA, formyl-CoA and formate as intermediates, and also reduction of oxalate to glyoxylate taking place via oxalyl-CoA. 3. The pink-pigmented organisms, when grown on oxalate, contain l-serine-glyoxylate aminotransferase and hydroxypyruvate reductase but do not contain glyoxylate carboligase. The converse of this obtains in oxalate-grown Ps. oxalaticus. This indicates that, in contrast with Ps. oxalaticus, synthesis of C(3) compounds from oxalate by the pink-pigmented organisms occurs by a variant of the ;serine pathway' used by Pseudomonas AM1 during growth on C(1) compounds. 4. Evidence in favour of this scheme is provided by the finding that a mutant of Pseudomonas AM1 that lacks hydroxypyruvate reductase is not able to grow on oxalate.

"Methylobacterium ethanolicum": a Syntrophic Association of Two Methylotrophic Bacteria

“…1 . 1 .29) (Large & Quayle, 1963) ; serine-glyoxylate aminotransferase (L-serine : glyoxylate aminotransferase, EC 2.6.1.45) (Blackmore & Quayle, 1970); methanol dehydrogenase (EC 1.1.99.8) (O'Connor & Hanson, 1977); hexulose phosphate synthase (Dahl et al, 1972); ribulosebisphosphate carboxylase [3-phospho-~-glycerate carboxy-lyase (dimerizing), EC 4.1.1.391 (Tabita et al, 1978).…”

Aerobic and Anaerobic Metabolism of Trimethylamine, Dimethylamine and Methylamine in Hyphomicrobium X

“…Hydroxypyruvate reductase was assayed by the method of Blackmore & Quayle (1970), except that 50 mwpotassium phosphate pH 7-0 was used as a buffer. …”

Hydroxypyruvate Reductase Activity in Paracoccus denitrificans

“…been used to furnish coupling enzyme(s) for measurement of oxaloacetate or hydroxypyruvate production, especially when use of NADPH can circumvent high levels of NADH oxidase activity (Blackmore & Quayle, 1970;Harder & Quayle, 1971 b). The present work shows that the greatest activity of NADPH-linked oxaloacetate reduction in crude extracts is due to malate dehydrogenase which can use either NAD+ or NADPf; at pH 7.0, the former coenzyme gives rates of reaction four-to fivefold higher than the latter.…”

“…Extracts of Paracoccus denitrificans grown on several carbon substrates contain an apparent pyridine nucleotide-linked hydroxypyruvate reductase activity for which there is no obvious metabolic role (Gibbs, 1966;Blackmore & Quayle, 1970;Cox & Quayle, 1975).…”