Ornithine transaminase from Cucurbita maxima cotyledons |
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| Authors: | W.E. Splittstoesser L. Fowden |
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| Affiliation: | Department of Horticulture, University of Illinois, Urbana, IL 61808, U.S.A.;Department of Botany and Microbiology, University College London, Gower Street, London WC1E 6BT U.K. |
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| Abstract: | During germination a marked increase in both soluble and particulate ornthine transaminase occurs in pumpkin cotyledons. Both enzymes had a pH optimum of 8.3 and a requirement for ornthine and α-ketoglutarate. Other keto acids or amino donors showed little activity. The enzymes required an active sulphydryl group for maximum activity. Exogenous pyridoxal phosphate was not required, but hydroxylamine inhibited the reaction and added pyridoxal phosphate overcame this inhibition. Proline inhibited the reaction and may play a role in the fate of ornithine in pumpkin cotyledons. |
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| Keywords: | Cucurbitaceae pumpkin amino acid inhibitors. |
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