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J Bacteriol. 1975 March; 121(3): 1022-1035

Metabolic control of urea catabolism in Chlamydomonas reinhardi and Chlorella pyrenoidosa.

ABSTRACT

In the unicellular green alga Chlamydomonas reinhardi (strain y-1), synthesis of the enzymes required for urea hydrolysis is under substrate induction control by urea and under end product repression control by ammonia. Hydrolysis of urea if effected by the sequential action of the discrete enzymes urea carboxylase and allophanate lyase, collectively called urea amidolyase. The carboxylase converts urea to allophanate in a reaction requiring biotin, adenosine 5'-triphosphate, and Mg2+. The lyase hydrolzyes allophanate to ammonium ions and bicarbonate. Neither activity is present in more than trace amounts when cultures are grown with ammonia or urea plus ammonia, or when they are starved for nitrogen for 8 h. Urea in the absence of ammonia induces both activities 10 to 100 times the basal levels. Addition of ammonia to an induced culture causes complete cessation of carboxylase accumulation and an 80% depression of lyase accumulation. Ammonia does not reduce urea uptake by repressed cells, so it does not prevent induction by the mechanism of inducer exclusion. The unicellular green alga Chlorella pyrenoidosa (strain 3 Emerson) also has discrete carboxylase and lyase enzymes, but only the carboxylase exhibits metabolic control.

This article has been cited by other articles:

• Shapir, N., Cheng, G., Sadowsky, M. J., Wackett, L. P. (2006). Purification and Characterization of TrzF: Biuret Hydrolysis by Allophanate Hydrolase Supports Growth. Appl. Environ. Microbiol. 72: 2491-2495 [Abstract] [Full Text]