Literature summary for 2.3.1.161 extracted from

Ma, S.M.; Li, J.W.; Choi, J.W.; Zhou, H.; Lee, K.K.; Moorthie, V.A.; Xie, X.; Kealey, J.T.; Da Silva, N.A.; Vederas, J.C.; Tang, Y.
Complete reconstitution of a highly reducing iterative polyketide synthase (2009), Science, 326, 589-592.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Saccharomyces cerevisiae	Aspergillus terreus

Organism

Organism	UniProt	Comment	Textmining
Aspergillus terreus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Aspergillus terreus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+	accessory protein LovC is needed: Loading of the megasynthase by malonyl-CoA is presumably followed by decarboxylation to yield the acetyl starter unit. Each round of Claisen condensation is catalyzed by the KS domain, whereas the growing polyketide is tethered to the phosphopantetheinyl arm of the ACP. After each condensation, the polyketide is subjected to a different combination of tailoring, which can include alpha-methylation by the MT domain, beta-ketoreduction by the KR domain, beta-dehydration by the DH domain, and alpha-beta-enoylreduction by the dissociated LovC. The different tailoring permutations after each round of chain extension yield a triene-containing hexaketide thioester that can undergo a stereospecific Diels-Alder cyclization to yield the decalin portion. After formation of the nonaketide, the chain is released to yield the ring-open form. In the absence of LovC, methylated hexa- and heptaketide pyrones are the primary products.	Aspergillus terreus	dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O	-	ir

Synonyms

Synonyms	Comment	Organism
lovastatin nonaketide synthase	-	Aspergillus terreus
LovB	-	Aspergillus terreus

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Aspergillus terreus
S-adenosyl-L-methionine	-	Aspergillus terreus

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Release 2023.1 (January 2023)