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- W1985890261 abstract "An acetohydroxy acid synthetase which synthesizes α-acetolactate from pyruvate has been isolated from the insoluble fraction of Neurospora crassa homogenates. A purification of about 200-fold was achieved by ammonium sulfate fractionation and the use of Sephadex and Sephadex-DEAE columns. It was shown that the purified enzyme is most active in the presence of Mn2+, and requires thiamine pyrophosphate for activity. About 10−1m pyruvate is necessary to give half maximal velocity. It has a pH optimum of about 6.1. It is not inhibited by valine, isoleucine, leucine, or pantothenate either singly or in concert. The enzyme also synthesizes acetoin in the presence of pyruvate plus acetaldehyde. In addition it synthesizes α-aceto-α-hydroxybutyrate in the presence of α-ketobutyrate plus pyruvate. The α-ketobutyrate is, however, inhibitory to the enzyme in increasing concentrations." @default.
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- W1985890261 date "1968-10-01" @default.
- W1985890261 modified "2023-09-27" @default.
- W1985890261 title "An acetohydroxy acid synthetase from Neurospora crassa" @default.
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- W1985890261 doi "https://doi.org/10.1016/0003-9861(68)90021-0" @default.
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