Ornithine carbamoyltransferase from Pyrococcus furiosus
Legrain, C.; Villeret, V.; Roovers, M.; Tricot, C.; Clantin, B.; Van Beeumen, J.; Stalon, V.; Glansdorff, N. (2001). Ornithine carbamoyltransferase from Pyrococcus furiosus. Methods Enzymol. 331: 227-235. https://dx.doi.org/10.1016/S0076-6879(01)31061-3
In: Methods in enzymology. Academic Press: New York. ISSN 0076-6879; e-ISSN 1557-7988, more
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| Authors | | Top |
- Legrain, C.
- Villeret, V.
- Roovers, M.
- Tricot, C.
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- Clantin, B.
- Van Beeumen, J.
- Stalon, V.
- Glansdorff, N.
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| Abstract |
Ornithine carbamoyltransferase (OTCase) catalyzes the conversion of ornithine and carbamoyl phosphate into citrulline in the de novo pathway for arginine synthesis or in the detoxifying urea cycle. In some microorganisms, an OTCase catalyzes the reverse reaction in the deiminase pathway for arginine degradations. Most anabolic OTCases are homotrimeric proteins containing three active sites, each one being formed by two adjacent monomers, whereas catabolic OTCases frequently contain more than three subunits. However, the OTCase of the hyperthermophilic archaeon Pyrococcus furiosus is dodecameric and nevertheless appears to fulfill a biosynthetic function; indeed, the host organism grows on a defined medium with ornithine as arginine precursor and genome analysis does not reveal any other OTCase gene or any sequence similar to known arginine deiminase determinants. |
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