EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   2.4.1.212 | -999 |
- |
more |
availability of substrate UDP-GlcNAc does not considerably influence the Km of Has1 toward UDP-GlcUA, whereas levels of UDP-GlcUA have a significant effect of the Km toward UDP-GlcNAc |
736145 |
| 2.4.1.212 | -999 |
- |
more |
kinetics, kinetic analysis of Cys-deletion mutants, overview |
659171 |
| 2.4.1.212 | -999 |
- |
more |
kinetics, wild-type and mutant enzymes |
658841 |
| 2.4.1.212 | -999 |
- |
more |
Km values of the enzyme in standard reaction in presence of diverse protecting nucleotide compounds, overview |
659175 |
| 2.4.1.212 | -999 |
- |
more |
recombinant enzyme, kinetics at different pH, thermodynamics |
658093 |
| 2.4.1.212 | -999 |
- |
more |
structural and kinetic analysis and modeling, both NAc- and UA-transferase domains follow a sequential kinetic mechanism, most likely an ordered one in which the UDP-sugar donor binds first, followed by the HA oligosaccharide. After transfer of the sugar moiety, both products are released, first the elongated HA oligosaccharide and then the UDP sugar. A mechanistic shift from a steady-state ordered bi-bi to rapid equilibrium ordered bi-bi mechanism is observed at the NAc-site between the HA6 and HA8 elongation, detailed overview |
736643 |
| 2.4.1.212 | -999 |
- |
more |
values for other substrate concentrations |
395251 |
| 2.4.1.212 | 0.014 |
- |
UDP-alpha-D-glucuronate |
25°C, pH 7.5 |
671308 |
| 2.4.1.212 | 0.032 |
- |
UDP-D-glucuronate |
HAS2 |
395251 |
| 2.4.1.212 | 0.034 |
- |
UDP-D-glucuronate |
HAS3 |
395251 |
