Purification, identification, and cloning of lysoplasmalogenase, the enzyme that catalyzes hydrolysis of the vinyl ether bond of lysoplasmalogen*

HIGHLIGHTS

• who: Lai-Chu Wu from the cellLysoplasmalogen substrates were prepared in liposomes at concentrations that might be found in cell membranes (, mol %). The lower two curves of Fig. , show that the purified enzyme catalyzed the hydrolysis of both substrates, albeit at lower rates compared with reactions in which the substrates were presented as aqueous suspensions (upper two curves). The substrate selectivity of lysoplasmalogenase was further investigated with, alkenyl-2-acyl-sn-glycero-3-phosphocholine or, alkenyl-2-acyl-sn-glycero-3-phosphoethanolamine, acyl-sn-glycero-3-phosphocholine or, acyl-sn-glycero-3phosphoethanolamine, and LPA. Enzyme assay B . . .
  

   

  

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