EC Number   |
|---|
    2.3.3.10 | bound covalently via Cys 117 to inhibitor (E,E)-11-(3-hydroxymethyl-4-oxo-2-oxytanyl)-3,5,7-trimethyl-2,4-undecadienoic acid, and in complex with acetyl-CoA and hydroxymethylglutaryl-CoA |
| 2.3.3.10 | in complex with (S)-3-hydroxy-3-methylglutaryl-CoA, sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M Bis-Tris (pH 6.5), 25% (w/v) PEG 3350, at 20°C |
| 2.3.3.10 | in complex with Co-A, sitting drop vapor diffusion method, using 0.1 M Bis-Tris (pH 6.5), 25% (w/v) polyethylene glycol (PEG) 3350, 0.2 M ammonium sulfate, at 4°C |
| 2.3.3.10 | in complex with hymeglusin, hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 6.3-6.5), 0.2 M NaCl, and 23% (w/v) polyethylene glycol 3350 |
| 2.3.3.10 | mutant A110G. Amide nitrogen of mutants S308 shifts 0.4 A toward the catalytic site cysteine residue stabilizing the intermediate negative charge. The hydroxyl group of S308 rotates to a position where it is able to stabilize the carbanion intermediate of the acetyl-S-enzyme during its condensation with acetoacetyl-CoA |
| 2.3.3.10 | sitting drop method, 18-20°C. The crystal structure of the native complex revealed a unique, shared CoA-binding site formed by both the acetoacetyl-CoA thiolase and 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase subunits thiolases (thiolases). A small scaffold protein connects the two enzymes |
| 2.3.3.10 | sitting-drop vapor-diffusion method, crystal structures of MvaS, the HMGCS from Myxococcus xanthus, in complex with CoA and acetylated active site Cys115, with the second substrate acetoacetyl CoA and with the product of the condensation reaction, 3-hydroxy-3-methylglutaryl CoA |
| 2.3.3.10 | sitting-drop vapour-diffusion method, crystal strcuture of full-length enzyme expressed in Escherichia coli is determined at 2.0 A resolution, crystal structure of HMG-CoA synthase with acetoacetyl-CoA is determined at 2.5 A resolution |
| 2.3.3.10 | unliganded and in complex with its second substrate/inhibitor acetoacetyl-CoA. The acetoacetyl-CoA binary structure demonstrates reduced coenzyme A and acetoacetate covalently bound to the active site cysteine through a thioester bond |
