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

Leukotriene A4 hydrolase in human leukocytes. Purification and properties.

Leukotriene A4 hydrolase, a soluble enzyme catalyzing hydrolysis of the allylic epoxide leukotriene A4 to the dihydroxy acid leukotriene B4, was purified to apparent homogeneity from human leukocytes. The enzymatic reaction obeyed Michaelis-Menten saturation kinetics with respect to varying concentrations of leukotriene A4. An apparent KM value ranging between 20 and 30 microM was deduced from Eadie-Hofstee plots. Physical properties including molecular weight (68,000-70,000), amino acid composition, and aminoterminal sequence were determined. It was indicated that leukotriene A4 hydrolase is a monomeric protein, distinct from previously described epoxide hydrolases in liver.[1]

References

  1. Leukotriene A4 hydrolase in human leukocytes. Purification and properties. Rådmark, O., Shimizu, T., Jörnvall, H., Samuelsson, B. J. Biol. Chem. (1984) [Pubmed]
 
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