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Laliberté G, Hellebust JA. Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only. Plant Physiol. 1990;93(1):62-6doi: 10.1104/pp.93.1.62.
Laliberté, G., & Hellebust, J. A. (1990). Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only. Plant physiology, 93(1), 62-6. https://doi.org/10.1104/pp.93.1.62
Laliberté, G, and Hellebust, J A. "Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only." Plant physiology vol. 93,1 (1990): 62-6. doi: https://doi.org/10.1104/pp.93.1.62
Laliberté G, Hellebust JA. Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only. Plant Physiol. 1990 May;93(1):62-6. doi: 10.1104/pp.93.1.62. PMID: 16667466; PMCID: PMC1062467.
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Plant Physiol. 1990 May;93(1):62-6. doi: 10.1104/pp.93.1.62.

Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only.

Plant physiology

G Laliberté, J A Hellebust

Affiliations

  1. Earth Sciences Centre, Department of Botany, University of Toronto, Toronto, Ontario, Canada, M5S 3B2.

PMID: 16667466 PMCID: PMC1062467 DOI: 10.1104/pp.93.1.62

Abstract

Although the existence of isozymes of ornithine carbamoyltransferase (carbamoylphosphate:l-ornithine carbamoyltransferase, EC 2.1.3.3) in higher plants has been reported, and the possibility exists that one or more of these operates catabolically to produce ornithine and carbamoylphosphate from citrulline and inorganic phosphate, no proof has been forthcoming. In view of the fact that many unicellular algae degrade arginine via arginine deiminase to citrulline and ammonium, and that the pathway of utilization of citrulline is unknown, we decided to investigate the possibility of the presence of a catabolic form of ornithine carbamoyltransferase in three microalgae known to have arginine deiminase activity. These were Chlorella autotrophica, Chlorella saccharophila, and Dunaliella tertiolecta. Our results show that the properties of OCT from these three algae are similar to OCTs from many higher plants with respect to general kinetics (K(m) values for ornithine and carbamoylphosphate), substrate inhibition by ornithine at high pHs, apparent sequential ordered kinetic mechanisms and paucity of apparent regulatory properties. Our data indicate an exclusively anabolic role of ornithine carbamoyltransferase in these algae.

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