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Uroporphyrinogen III synthase: Studies on its mechanism of action, molecular biology and biochemistry

✍ Scribed by Nigel Crockett; Peter R Alefounder; Alan R Battersby; Chris Abell

Publisher: Elsevier Science
Year: 1991
Tongue: French
Weight: 949 KB
Volume: 47
Category: Article
ISSN: 0040-4020
DOI: 10.1016/s0040-4020(01)86492-9

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✦ Synopsis

A review is given of studies on the mechanism of action of uroporphyrinogen III syntbase (cosynthetase, EC 4.2.1.75) based on synthesis of an inhibitory spiro-lactarn. HemD, the Escherichiu coli gene coding for uroporphyrinogen Ill synthase has been cloned and overexpressed at levels sixteen fold higher than in wild type E. coli. Evidence for hemD being part of an operon is reviewed. Uroporphyrinogen III synthase, which has been purified approx. 6000 fold, shows Mr 28000 under denaturing conditions and has a pH optimum of 8.0 f 0.2. The results from chemical modification of the enzyme point to the presence of arginine and lysine residues at or close to the active site.

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