Literature summary for 2.3.1.94 extracted from

Koryakina, I.; Kasey, C.; McArthur, J.B.; Lowell, A.N.; Chemler, J.A.; Li, S.; Hansen, D.A.; Sherman, D.H.; Williams, G.J.
Inversion of extender unit selectivity in the erythromycin polyketide synthase by acyltransferase domain engineering (2017), ACS Chem. Biol., 12, 114-123 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	development of mutations that shift the extender unit selectivity of the DEBS terminal module Ery6 (lacking a TE domain) towards either extender unit 2-methylmalonyl-CoA or (prop-2-yn-1-yl)propanedioyl-CoA. Mutants are able to use non-natural alkynyl-modified extender units while maintaining more than twice the activity of the wild-type with its natural substrate	Saccharopolyspora erythraea
V187A/Y189R	mutant is able to utilize non-natural alkynyl-modified extender units	Saccharopolyspora erythraea
Y189R	mutant produces the propargyl analogue of 10-deoxymethynolide as the major product, while the wild-type enzyme prefers the natural substrate 2-methylmalonyl-CoA to provide the natural macrolactone 10-deoxymethynolide as the major product	Saccharopolyspora erythraea

Organism

Organism	UniProt	Comment	Textmining
Saccharopolyspora erythraea	Q03133	6-deoxyerythronolide-B synthase EryA3, modules 5 and 6	-

Synonyms

Synonyms	Comment	Organism
DEBS3	-	Saccharopolyspora erythraea

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Release 2023.1 (January 2023)