EC Number   |
Reference |
|---|
    2.5.1.61 | - |
489947 |
| 2.5.1.61 | molecular dynamics simulations reveal that the HMBS active-site loop movement and cofactor turn create space for the elongating pyrrole chain. Twenty-seven residues around the active site and water molecules interact to stabilize the large, negatively charged, elongating polypyrrole. Residues R26 and R167 are the strongest candidates for proton transfer to deaminate the incoming porphobilinogen molecules. R167 is a gatekeeper and facilitator of hydroxymethylbilane egress through the space between the enzyme's domains and the active-site loop |
760071 |
| 2.5.1.61 | network analysis identifies 13 structural clusters persistent across five molecular dynamics trajectories corresponding to the five steps of pyrrole polymerization, which are responsible for maintaining the tertiary structure and domain arrangements of the enzyme. Amino acid residues R26 and F77 regulate the active site loop movement across the stages |
759637 |
| 2.5.1.61 | purified recombinant detagged enzyme, mixing of 2.5 mg/ml protein with 0.1 M sodium cacodylate, pH 6.5-6.8, 0.2 M magnesium acetate, and 25-30%PEG 8000, room temperature, removal of the His tag is necessary to obtain enzyme crystals, X-ray diffraction structure determination and analysis at 1.46-1.60 A resolution |
737372 |
| 2.5.1.61 | purified recombinant detagged enzyme, mixing of 2.5 mg/ml protein with 0.1 M sodium cacodylate, pH 6.5-6.8, 0.2 M magnesium acetate, and 25-30%PEG 8000, X-ray diffraction structure determination and analysis at 1.46-1.60 A resolution |
737348 |
| 2.5.1.61 | purified recombinant enzyme with bound cofactor, crystallization in the dark due to light-sensitivity of the cofactor, hanging drop method, mixing of 5 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 5 mM DTT, with reservoir solution containing 25% w/v PEG 4000, 100 mM sodium citrate, pH 5.6, and 200 mM ammonium sulfate, X-ray diffraction structure determination and analysis at 1.45 A resolution, molecular modelling |
737341 |
| 2.5.1.61 | SeMet-labelled enzyme |
489949 |
| 2.5.1.61 | vapor diffusion method, hanging drops with 20 mM Tris-HCl buffer, pH 8.2, containing 5 mM dithiothreitol and reservoir solution consisting of 0.6 M ammonium sulfate, 1.2 M lithium sulfate, 5% ethylene glycol, 50 mM sodium citrate, pH 5.6, and 50 mM dithiothreitol, diffraction data are collected at -173°C in 30% glycerol cryoprotected protein crystals |
707428 |
