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B6db references: 91054346

type Journal Article
authors Schaeffer, J. M.; Donatelli, M. R.
title Characterization of a high-affinity membrane-associated ornithine decarboxylase from the free-living nematode Caenorhabditis elegans
journal Biochem J
ui 91054346
year (1990)
volume 270
number 3
pages 599-604.
keywords Amino Acids/pharmacology
abstract Ornithine decarboxylase has been identified and characterized in the free-living nematode Caenorhabditis elegans. Unlike previously described ornithine decarboxylases, the enzyme activity is membrane- associated and remains in the membrane fraction after treatment with high salt, detergents or phosphatidylinositol-specific phospholipase C. Ornithine has an apparent Km value of 2.7 microM for ornithine decarboxylase. The enzyme is competitively inhibited by arginine and lysine with Ki values of 4.0 and 24.4 microM respectively. None of the other naturally occurring amino acids inhibited more than 10% of the enzyme activity at concentrations up to 1 mM. Agmatine, putrescine, spermidine and spermine inhibit ornithine decarboxylase in a non- competitive manner with Ki values of 10, 53.5, 59 and 855 microM respectively. A similar ornithine decarboxylase activity was also identified in membrane preparations from the parasitic nematode Haemonchus contortus.
last changed 2002/11/12 16:17

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