EC 1.14.13.198      
Transferred entry: monacolin L hydroxylase. Now EC 1.14.14.125, monacolin L hydroxylase
[EC 1.14.13.198 created 2014, deleted 2018]
 
 
EC 1.14.14.125     
Accepted name: monacolin L hydroxylase
Reaction: monacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = monacolin J acid + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: monacolin L acid = (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
monacolin J acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
Other name(s): LovA (ambiguous)
Systematic name: monacolin L acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from fungi also catalyses the reaction of EC 1.14.14.124, dihydromonacolin L hydroxylase.
References:
1.  Barriuso, J., Nguyen, D.T., Li, J.W., Roberts, J.N., MacNevin, G., Chaytor, J.L., Marcus, S.L., Vederas, J.C. and Ro, D.K. Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA. J. Am. Chem. Soc. 133 (2011) 8078–8081. [PMID: 21495633]
[EC 1.14.14.125 created 2014 as EC 1.14.13.198, transferred 2018 to EC 1.14.14.125]
 
 
EC 2.3.1.238     
Accepted name: monacolin J acid methylbutanoate transferase
Reaction: monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] = lovastatin acid + [2-methylbutanoate polyketide synthase]
Glossary: monacolin J acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
lovastatin acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-2,6-dimethyl-8-{[(2S)-2-methylbutanoyl]oxy}-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LovD
Systematic name: monacolin J acid:(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] (S)-2-methylbutanoate transferase
Comments: The enzyme catalyses the ultimate reaction in the lovastatin biosynthesis pathway of the filamentous fungus Aspergillus terreus.
References:
1.  Kennedy, J., Auclair, K., Kendrew, S.G., Park, C., Vederas, J.C. and Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284 (1999) 1368–1372. [PMID: 10334994]
2.  Xie, X., Watanabe, K., Wojcicki, W.A., Wang, C.C. and Tang, Y. Biosynthesis of lovastatin analogs with a broadly specific acyltransferase. Chem. Biol. 13 (2006) 1161–1169. [PMID: 17113998]
3.  Xie, X., Meehan, M.J., Xu, W., Dorrestein, P.C. and Tang, Y. Acyltransferase mediated polyketide release from a fungal megasynthase. J. Am. Chem. Soc. 131 (2009) 8388–8389. [PMID: 19530726]
[EC 2.3.1.238 created 2014]
 
 


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