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EC Number General Information Commentary Reference
Show all pathways known for 2.3.1.94Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.94more enzyme-substrate interactions are involved in the translocation of a polyketide from ACP2 to ketosynthase KS3, the ACP domain of the 6-deoxyerythronolide B synthase contributes to its association with its ketosynthase, KS, translocation partner, models for KS-ACP recognition during chain elongation and chain translocation, docking model, overview. Determination of selective protein–protein interactions between the two partners using CF3-S-ACP as probe. The acyl chain substrate also has a significant influence on this interaction 720991
Show all pathways known for 2.3.1.94Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.94physiological function ketoreductases from DEBS modules 2 and 5 display little preference for oxidation of substrates tethered to their cognate ACP domains over those attached to the other ACP domains tested. The ketoreductase from DEBS module 1 shows an about 10-50fold preference for substrate attached to its native ACP domain, whereas the ketoreductase from DEBS module 6 displays an about 10fold preference for the ACP from DEBS module 5 757075
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