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Partial Purification and Properties of Ornithine Transcarbamoylase from Nostoc muscorum Kützing ¹

^a Department of Botany, Duke University, Durham, North Carolina 27706

Ornithine transcarbamoylase (carbamoyl phosphate:L-ornithine carbamoyltransferase, EC 2.1.3.3) has been partially purified from the blue-green alga Nostoc muscorum Kützing, an organism in which the enzyme seems to be involved in a bicarbonate-fixing pathway leading to citrulline. Pertinent to possible regulation of this pathway, the enzyme shows hyperbolic substrate kinetics, has a molecular weight estimated at 75,000 daltons, and its catalytic capability is little influenced by a selection of metabolites that might conceivably act as regulators in vivo. Thus it seems unlikely that this enzyme is the control point for bicarbonate fixation. In terms of energy of activation (12.3 kcal/mole), size and Km for carbamoylphosphate, the Nostoc enzyme resembled preparations from liver and higher plants more than preparations from Streptococcus and Mycoplasma. The enzymes from Streptococcus and Mycoplasma are probably specialized for citrulline breakdown rather than citrulline synthesis. The Km for ornithine was 2.5 mM at a saturating concentration of carbamoylphosphate and the Km for carbamoylphosphate was 0.7 mM at an ornithine concentration of 2 mM. Ornithine was inhibitory at concentrations greater than 2 mM. Phosphate was a competitive inhibitor with respect to carbamoylphosphate. The pH optimum for citrulline synthesis was 9.5.

¹ Financial support was provided by National Science Foundation Grant GB-34117 to A.W.N. and a National Defense Education Act Title IV fellowship followed by a National Science Foundation Predoctoral Fellowship to S.F.B.