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EC Number Crystallization (Commentary) Reference
Display the reaction diagram Show all sequences 2.3.1.201hanging drop vapor diffusion method. The enzyme complexed with acetyl-CoA and UDP is crystallized at pH 8.0 in the presence of 100 mM HEPPS, 16-20% (w/v) poly(ethylene glycol) 3400 and 210 mM tetramethylammonium chloride. The enzyme bound to CoA and UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate is crystallized using 17% (w/v) poly(ethylene glycol) 3400, 300 mM NaCl, 100 mM HEPPS (pH 8.0), 210 mM tetramethylammonium chloride 718872
Display the reaction diagram Show all sequences 2.3.1.201QM/MM calculations reveal two sequential steps in the catalyzation process. The nucleophilic attack of the C3-amino group of the substrate on the carbonyl carbon of acetyl-CoA occurs in concert with the departure of CoA from acetyl-CoA, generating a negatively charged CoA and a positively charged intermediate. Subsequently, the sulfur anion of CoA accepts the proton of the positively charged intermediate to yield the final product. Asn84 is important for promoting the catalysis by forming a hydrogen bond with the C3-amino group to position the lone pair of the electrons of the C3-amino group in an ideal orientation for nucleophilic attack and stabilize the transition states and intermediate 737234
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