Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7. Lolines are structurally differentiated by the various modifications of the L-amino group and include norloline, loline, N-methylloline, N-acetylloline, N-acetylnorloline, and N-formylloline. The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP. Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo-acetamidopyrrolizidine (AcAP). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo-acetamidopyrrolizidine (AcAP). In sequential 2-oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines. The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation. Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines. LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N-methyllonine (NML) by lolM. LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL). A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL). LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of L-homoserine from L-aspartate