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Results 1 - 4 of 4
EC Number
Subunits
Commentary
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domain architecture, the enzyme shows an alpha/beta-hydrolase fold in the catalytic closed form with a distinct hydrophobic substrate-binding chamber involving the PksA thioesterase/Claisen cyclase residues Ser1937, His2088, and Asp1964, which constitute the catalytic triad conserved in the alpha/beta-hydrolase family, detailed overview
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domain organization of PksA with acyl-carrier protein (ACP), acyl transacylase (AT), dehydrase (DH), enoyl reductase (ER), ketoreductase (KR), ketoacyl synthase (KS), pseudomethyltransferase (PsiMT), starter unit:ACP transacylase (SAT), and thioesterase (TE), structure model, overview
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domain structure, and dissection of domains, interactions, overview
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PksA domain structure, from N- to C-terminus including the starter unit: acylcarrier protein transacylase (SAT), beta-ketoacyl synthase (KS), malonyl-CoA: acyl-carrier protein transacylase (MAT), product template (PT), acyl-carrier protein (ACP), and thioesterase/Claisen cyclase (TE/CLC)
Results 1 - 4 of 4