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Science 28 October 1966:
Vol. 154. no. 3748, pp. 501 - 503
DOI: 10.1126/science.154.3748.501

Articles

Coordinate Synthesis of Heme and Apoenzyme in the Formation of Tryptophan Pyrrolase

Harvey S. Marver 1, Donald P. Tschudy 1, Mark G. Perlroth 1, and Annie Collins 1

1 Metabolism Branch, National Cancer Institute, Bethesda, Maryland 20014

Reciprocal control mechanisms between hemoprotein and 8-aminolevulinic acid synthetase take part in coordinate synthesis of the heme and apoenzyme moieties of tryptophan pyrrolase. Stimulation of heme biosynthesis increases tryptophan pyrrolase, whereas enhancement of heme binding by apotryptophan pyrrolase secondarily increases the formation of dgr-aminolevulinic acid synthetase, the rate-limiting enzyme in heme formation. Tryptophan-mediated induction of dgr-aminolevulinic acid synthetase suggests that heme participates in repression of that enzyme


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