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- W2013111386 abstract "Abstract The first enzyme of the sphingolipid pathway has been purified >100 times. The enzyme has an apparent M r of 66,500. The partially purified enzyme was used to determine K m for serine (1.13 m m ); the apparent K m for palmitoyl CoA was anomalous. The pH optimum of the synthetase was found between pH 7.0 and 7.6. The effectiveness of various acyl CoAs was related to chain length showing a symmetrical distribution around C 16 (palmitoyl). Decanoyl CoA was the shortest compound showing activity. The unsaturated C 18 , (oleoyl) CoA, showed significantly reduced activity as compared with stearoyl CoA. A number of compounds which inhibited synthetase activity were examined; cysteine competitively inhibited the response of the enzyme to serine ( K i = 0.49 mM) and a number of halogens were inhibitory in the order I = Br > Cl > F. Thiocyanate was a potent inhibitor of 3KDS synthetase (70% inhibition at 1 m m ). The response of the apoenzyme to its cofactor pyridoxal phosphate was linear from 0 → 10 μ m and reached a maximum between 10 and 20 μ m . In extracts from mid-log-phase cells, approximately 50% of the synthetase exists in the apoenzyme form." @default.
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- W2013111386 date "1981-12-01" @default.
- W2013111386 modified "2023-09-26" @default.
- W2013111386 title "The 3-ketodihydrosphingosine synthetase of Bacteroides melaninogenicus: Partial purification and properties" @default.
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- W2013111386 doi "https://doi.org/10.1016/0003-9861(81)90384-2" @default.
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