Literature summary for 2.3.1.240 extracted from

Whicher, J.R.; Dutta, S.; Hansen, D.A.; Hale, W.A.; Chemler, J.A.; Dosey, A.M.; Narayan, A.R.; Hakansson, K.; Sherman, D.H.; Smith, J.L.; Skiniotis, G.
Structural rearrangements of a polyketide synthase module during its catalytic cycle (2014), Nature, 510, 560-564.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Streptomyces venezuelae

Organism

Organism	UniProt	Comment	Textmining
Streptomyces venezuelae	Q9ZGI5 and Q9ZGI4 and Q9ZGI3 and Q9ZGI2 and Q9ZGI1	Q9ZGI5: type I polyketide synthase PikAI, Q9ZGI4: type I polyketide synthase PikAII, Q9ZGI3: type I polyketide synthase PikAIII, Q9ZGI2: type I polyketide synthase PikAIV, Q9ZGI1: thioesterase II PikAV. Multifunctional, modular enzyme	-
Streptomyces venezuelae ATCC 15439	Q9ZGI5 and Q9ZGI4 and Q9ZGI3 and Q9ZGI2 and Q9ZGI1	Q9ZGI5: type I polyketide synthase PikAI, Q9ZGI4: type I polyketide synthase PikAII, Q9ZGI3: type I polyketide synthase PikAIII, Q9ZGI2: type I polyketide synthase PikAIV, Q9ZGI1: thioesterase II PikAV. Multifunctional, modular enzyme	-

Purification (Commentary)

Purification (Comment)	Organism
-	Streptomyces venezuelae

Reaction

Reaction	Comment	Organism	Reaction ID
malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O	electron cryo-microscopy (cryo-EM) structures of a full-length polyketide synthase module in three key biochemical states of its catalytic cycle reveals the dynamics of the intramodule acyl carrier protein for sequential binding to catalytic domains within the reaction chamber, and for transferring the elongated and processed polyketide substrate to the next module in the polyketide synthase pathway. During the enzymatic cycle the ketoreductase domain undergoes dramatic conformational rearrangements that enable optimal positioning for reductive processing of the acyl carrier protein-bound polyketide chain elongation intermediate	Streptomyces venezuelae	a

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Release 2023.1 (January 2023)