EC Number   |
Subunits |
Reference |
|---|
    2.7.6.3 | ? |
x * 18000, SDS-PAGE |
723713 |
| 2.7.6.3 | ? |
x * 54053, sequence calculation |
674784 |
| 2.7.6.3 | homodimer |
Arg79 and Gln88 may help to stabilize the homodimer. The long side chain of Arg79 in YpHPPK forms many hydrophobic interactions with Trp90 and Gln49 from the partner subunit and a weak hydrogen bond with the side chain of Gln49, which may help to stabilize the dimeric molecule |
695332 |
| 2.7.6.3 | monomer |
1 * 18299, calculation from nucleotide sequence |
642764 |
| 2.7.6.3 | monomer |
1 * 25000, SDS-PAGE |
639671 |
| 2.7.6.3 | monomer |
1 * 50509, the bifunctional enzyme HPPK-DHPS exists mainly as a monomer in solution, calculated from amino acid sequence |
-, 723522 |
| 2.7.6.3 | monomer |
1 * 53000, the bifunctional enzyme HPPK-DHPS exists mainly as a monomer in solution, sedimentation velocity and equilibrium analysis |
-, 723522 |
| 2.7.6.3 | More |
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis enzyme |
642760 |
| 2.7.6.3 | More |
the bifunctional protein 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase is involved in tetrahydrofolate synthesis |
639684 |
| 2.7.6.3 | More |
the enzyme has an alphabetaalpha fold with a central six-stranded beta-sheet sandwiched by two alpha-helices on either side |
737717 |
