Analysis of the control of citrulline synthesis in isolated rat-liver mitochondria

R. J. Wanders; C. W. van Roermund; A. J. Meijer

doi:https://doi.org/10.1111/j.1432-1033.1984.tb08278.x

Analysis of the control of citrulline synthesis in isolated rat-liver mitochondria

R. J. Wanders, C. W. van Roermund, A. J. Meijer

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Abstract

The amount of control of the various steps involved in the citrulline synthesizing pathway in isolated rat-liver mitochondria incubated with saturating concentrations of ammonia and ornithine has been measured. The flux control coefficient of carbamoyl-phosphate synthase (ammonia) was close to one. Control exerted by other steps in the pathway, including ornithine transcarbamoylase, carbonic anhydrase. ATP production and transport of ornithine, was negligible. The high flux control coefficient of carbamoyl-phosphate synthetase is due to the low elasticity coefficient of this enzyme towards its product, intramitochondrial carbamoyl phosphate, in combination with a high elasticity coefficient of ornithine transcarbamoylase towards carbamoyl phosphate

Original language	English
Pages (from-to)	247-254
Journal	European Journal of Biochemistry / FEBS
Volume	142
Issue number	2
DOIs	https://doi.org/10.1111/j.1432-1033.1984.tb08278.x
Publication status	Published - 1984

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https://doi.org/10.1111/j.1432-1033.1984.tb08278.x

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title = "Analysis of the control of citrulline synthesis in isolated rat-liver mitochondria",

abstract = "The amount of control of the various steps involved in the citrulline synthesizing pathway in isolated rat-liver mitochondria incubated with saturating concentrations of ammonia and ornithine has been measured. The flux control coefficient of carbamoyl-phosphate synthase (ammonia) was close to one. Control exerted by other steps in the pathway, including ornithine transcarbamoylase, carbonic anhydrase. ATP production and transport of ornithine, was negligible. The high flux control coefficient of carbamoyl-phosphate synthetase is due to the low elasticity coefficient of this enzyme towards its product, intramitochondrial carbamoyl phosphate, in combination with a high elasticity coefficient of ornithine transcarbamoylase towards carbamoyl phosphate",

author = "Wanders, {R. J.} and {van Roermund}, {C. W.} and Meijer, {A. J.}",

year = "1984",

doi = "https://doi.org/10.1111/j.1432-1033.1984.tb08278.x",

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journal = "European Journal of Biochemistry / FEBS",

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AU - Wanders, R. J.

AU - van Roermund, C. W.

AU - Meijer, A. J.

PY - 1984

Y1 - 1984

N2 - The amount of control of the various steps involved in the citrulline synthesizing pathway in isolated rat-liver mitochondria incubated with saturating concentrations of ammonia and ornithine has been measured. The flux control coefficient of carbamoyl-phosphate synthase (ammonia) was close to one. Control exerted by other steps in the pathway, including ornithine transcarbamoylase, carbonic anhydrase. ATP production and transport of ornithine, was negligible. The high flux control coefficient of carbamoyl-phosphate synthetase is due to the low elasticity coefficient of this enzyme towards its product, intramitochondrial carbamoyl phosphate, in combination with a high elasticity coefficient of ornithine transcarbamoylase towards carbamoyl phosphate

AB - The amount of control of the various steps involved in the citrulline synthesizing pathway in isolated rat-liver mitochondria incubated with saturating concentrations of ammonia and ornithine has been measured. The flux control coefficient of carbamoyl-phosphate synthase (ammonia) was close to one. Control exerted by other steps in the pathway, including ornithine transcarbamoylase, carbonic anhydrase. ATP production and transport of ornithine, was negligible. The high flux control coefficient of carbamoyl-phosphate synthetase is due to the low elasticity coefficient of this enzyme towards its product, intramitochondrial carbamoyl phosphate, in combination with a high elasticity coefficient of ornithine transcarbamoylase towards carbamoyl phosphate

U2 - https://doi.org/10.1111/j.1432-1033.1984.tb08278.x

DO - https://doi.org/10.1111/j.1432-1033.1984.tb08278.x

M3 - Article

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SN - 0014-2956

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SP - 247

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JO - European Journal of Biochemistry / FEBS

JF - European Journal of Biochemistry / FEBS

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