EC Number   |
Natural Substrates |
|---|
    2.7.7.4 | ATP + sulfate |
- |
| 2.7.7.4 | diphosphate + adenylyl sulfate |
- |
| 2.7.7.4 | ATP + sulfate |
adenylylsulfate transgenics are more tolerant than wild-type to As(III), As(V), Cd2+, Cu2+, Hg2+, and Zn2+, but less tolerant to Mo6+ and V6+. The APS seedlings has up to 2.5-fold higher shoot concentrations of As(III), As(V), Hg2+, Mo6+, Pb2+, and V6+, and somewhat lower Cr3+ levels. Mature APS plants contained up to 2.5fold higher shoot concentrations of Cd2+, Cr3+, Cu2+, Mo6+, V6+, and W than wild type. They also contain 1.5fold to 2fold higher levels of the essential elements Fe, Mo, and S in most of the treatments |
| 2.7.7.4 | ATP + sulfate |
catalyzes a reaction in the sulfate assimilation pathway. The chloroplast isoenzyme, representing the more abundant enzyme form, declines in parallel with APS reductase activity during aging of leaf. The cytosolic isoenzyme plays a specialized function that is probably unrelated to sulfate reduction. A plausible function could be in generating APS for sulfate reactions |
| 2.7.7.4 | more |
catalyzes the rate-limiting step in the assimilatory pathway for sulfate |
| 2.7.7.4 | ATP + sulfate |
constitutive enzyme |
| 2.7.7.4 | ATP + sulfate |
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system |
| 2.7.7.4 | ATP + sulfate |
enzyme plays a crucial role in sulfate activation |
| 2.7.7.4 | ATP + sulfate |
first enzyme of the two-step sulfate activation sequence |
| 2.7.7.4 | more |
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM |
