The vanadium chloroperoxidase from Curvularia inaequalis; some properties of the enzyme
β Scribed by J.W.P.M. van Schijndel; E.G.M. Vollenbrock; L.H. Simons; R. Wever
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 68 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0162-0134
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The enzymes of the leucine pathway of Candida maltosa were investigated and the regulatory pattern was established. L-leucine inhibited the a-isopropylmalate (IPM) synthase, the first enzyme of the pathway. The inhibition was competitive with respect to a-ketoisovalerate , (Ki = 0.81 mM) and non-com
Malate synthase, one of the key enzymes in the glyoxylate cycle, was purified from peroxisomes of alkanegrown yeast, Candida tropicalis. The enzyme was mainly localized in the matrix of peroxisomes, judging from subcellular fractionation followed by exposure of the organelles to hypotonic conditions