What question did this study set out to answer?

The aim was to purify ornithine carbamoyltransferase from E. coli W and investigate its enzyme mechanism kinetically.

March 1, 1976European Journal of BiochemistryOpen Access

Ornithine Carbamoyltransferase from Escherichia coli W

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Authors

CLChristiane LEGRAINCentre d'Enseignement et de Recherches des Industries Alimentaires et Chimiques VSVictor StalonUniversité Libre de Bruxelles

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Implication

Purification and kinetic analysis of ornithine carbamoyltransferase reveals its enzymatic mechanism in E. coli W, indicating significant insights into substrate interactions.

Key Points

The aim was to purify ornithine carbamoyltransferase from E. coli W and investigate its enzyme mechanism kinetically.
Purified ornithine carbamoyltransferase to homogeneity from E. coli W.
Studied the kinetic properties using product inhibition and dead-end inhibition.
Measured Michaelis and dissociation constants for enzymatic reactions.
Enzyme has a molecular weight of 105000 composed of three identical subunits of 35000 each.
Kinetic studies suggest a compulsory binding sequence with carbamoylphosphate as the first substrate.
The kinetic constants for forward and reverse reactions are of comparable magnitudes.

Cite This Study

LEGRAIN et al. (1976) studied this question.

synapsesocial.com/papers/6a7060e884cc45bb7bdfbfdf https://doi.org/10.1111/j.1432-1033.1976.tb10230.x

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Implication

Purification and kinetic analysis of ornithine carbamoyltransferase reveals its enzymatic mechanism in E. coli W, indicating significant insights into substrate interactions.

Ornithine Carbamoyltransferase from Escherichia coli W

Discussion

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Implication

Key Points

Cite This Study

Ornithine Carbamoyltransferase from Escherichia coli W

Discussion

Member takes

Implication

Key Points

Cite This Study

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