PMID:7451404
| Citation |
Fujita, Y, Shimakata, T and Kusaka, T (1980) Purification of two forms of enoyl-CoA hydratase from Mycobacterium smegmatis. J. Biochem. 88:1045-50 |
|---|---|
| Abstract |
Two forms of enoyl-CoA hydratase (hydratases I and II), which are different from each other in substrate specificity, were found in a crude extract of Mycobacterium smegmatis. Hydratase I was more active with crotonyl-CoA as a substrate than with decenoyl-CoA, whereas the reverse was the case for hydratase II. Hydratase I was purified 688-fold to homogeneity with a yield of 14.5% from the crude extract. Its molecular weight was estimated to be 16,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 30,000 by gel filtration, suggesting that the enzyme is dimeric. Hydratase II was also partially purified. The Vmax of hydratase I decreased progressively with increase in the carbon-chain length of the substrate from 2,488 units/mg for crotonyl-CoA to 154 units/mg for hexadecenoyl-CoA, whereas the Km values for crotonyl-CoA (82 microM), decenoyl-CoA (91 microM), and hexadecenoyl-CoA (105 microM) were similar. Both hydratases were inhibited by acetoacetyl-CoA and pCMS, but not by N-ethylmaleimide or monoiodoacetate. |
| Links | |
| Keywords |
Enoyl-CoA Hydratase/isolation & purification; Enoyl-CoA Hydratase/metabolism; Hydro-Lyases/isolation & purification; Kinetics; Molecular Weight; Mycobacterium/enzymology; Substrate Specificity |
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