Literature summary for 2.3.1.94 extracted from

Dunn, B.J.; Watts, K.R.; Robbins, T.; Cane, D.E.; Khosla, C.
Comparative analysis of the substrate specificity of trans- versus cis-acyltransferases of assembly line polyketide synthases (2014), Biochemistry, 53, 3796-3806.

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Organism

Organism	UniProt	Comment	Textmining
Saccharopolyspora erythraea	Q03131 and Q03132 and Q03133	Q03131, i.e. modules 1 and 2, Q03132, i.e. modules 3 and 4, Q03133, i.e. modules 5 and6	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the cis-acyltransferase domain from DEBS module 3 transfers a methylmalonyl extender unit from the corresponding carboxyacyl-CoA precursor onto the phosphopantetheine arm of the acyl carrier protein within the same module. The presence of the acyl carrier protein has little effect on the specificity of the cis-acyltransferase domain for carboxyacyl-CoA substrates, but has a marked influence on the corresponding specificity parameters for the trans-acyltransferases from the disorazole and kirromycin synthases. Comparative analysis of the substrate specificity	Saccharopolyspora erythraea	?	-	?
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+	-	Saccharopolyspora erythraea	6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+	-	?

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Release 2023.1 (January 2023)