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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Purification and properties of S-alkyl-L-cysteine lyase from seedlings of Acacia farnesiana Willd.

1. An S-alkyl-L-cysteine lyase (EC was purified to apparent homogeneity from extracts of acetone-dried powders of the hypocotyls of etiolated 5-day-old seedlings of Acacia farnesiana Willd. 2. The enzyme catalyses a beta-elimination reaction and will utilize both the thioether and sulphoxide form of the substrate. 3. There is a braod specificity with regard to the alkyl substituent, but cystathionine is utilized very poorly. 4. The pH optimum is 7.8 and the Km value for the probable natural substrate L-djenkolate is 0.3 mM. 5. Both sodium dodecyl sulphate-polyacrylamide-gel electrophoresis and ultracentirfugal analysis give a molecular weight of about 144000. 6. One mol of pyridoxal phosphate is bound/ mol of enzyme. 7. The energy of activation with L-djenkolate as the substrate is 53.1 kJ/ mol. 8. The enzyme has a partial specific volume of 0.56 and S20,w 7.26S.[1]


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