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. 1974 Nov;54(5):791–793. doi: 10.1104/pp.54.5.791

Microenvironmental Manipulation of the Observed Michaelis Constant of Ribulose Diphosphate Carboxylase 1

Louise E Anderson a
PMCID: PMC366605  PMID: 16658974

Abstract

Urease and ribulose 1, 5-diphosphate carboxylase can be bound to Sepharose to give an immobilized two-enzyme system which catalyzes the reaction urea → H2CO3 → phosphoglyceric acid. The observed Km of the system for urea approaches the lower value for urease when carboxylase levels on the gel exceed urease levels. If a similar system operates in the chloroplast, the high Km (H2CO3) of ribulose 1,5-diphosphate carboxylase may not be metabolically significant.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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