Rat liver ATP-sulfurylase: purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions.

@article{Yu1989RatLA,
  title={Rat liver ATP-sulfurylase: purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions.},
  author={Mingchao Yu and Robert L. Martin and S K Jain and L. Chen and Irwin H. Segel},
  journal={Archives of biochemistry and biophysics},
  year={1989},
  volume={269 1},
  pages={
          156-74
        }
}

Kinetic and Stability Properties of Penicillium chrysogenum ATP Sulfurylase Missing the C-terminal Regulatory Domain*

The cumulative results indicate that the more negative entropy of activation of the truncated enzyme for APS synthesis is consistent with a role of the C-terminal domain in promoting the effective orientation of MgATP and sulfate at the active site.

Human 3'-phosphoadenosine 5'-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains.

The (a) imbalance between ATP sulfurylase and APS kinase activities, (b) accumulation of APS in solution during the overall reaction, (c) rate acceleration provided by exogenous APS Kinase, and (d) availability of both active sites to exogenousAPS all argue against APS channeling.

Temperature effects on the allosteric transition of ATP sulfurylase from Penicillium chrysogenum.

The cumulative results indicate that increasing the temperature increases the allosteric constant, L, i.e., promotes a shift in the base-level distribution of enzyme molecules from the high MgATP affinity R state toward the low Mg ATP affinity T state, as a result of which the enzyme displays a true "temperature optimum" at subsaturating M gATP.

Induction of Positive Cooperativity by Amino Acid Replacements within the C-terminal Domain of Penicillium chrysogenum ATP Sulfurylase*

Both mutant enzymes were cleaved more rapidly than the wild type enzyme, suggesting that movement of the mobile loop occurs during the R to T transition.

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ATP sulfurylase from higher plants : purification and preliminary kinetics studies on the cabbage leaf enzyme.

Initial velocity and product inhibition studies of the forward and reverse reactions point to an obligately ordered kinetic mechanism with MgATP adding before MoO(4) (2-) and MgPPi leaving before AMP + MoO (4)(2-) (or adenosine-5'-phosphosulfate [APS]).

Purification and properties of the ATP sulphurylase of rat liver.