Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

KST-1A9127 [(1S,4S)-7,7-dimethyl-2,3- dioxo-1...

Synonyms: AC1L4PAI, CTK2H9622, AR-1A8036, FT-0623435, 73413-79-3, ...

Dailey, H.A. et al., Schasteen, C.S. et al., Pearson, R.B. et al.

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High impact information on Camphorquinone-10-sulfonic acid

Comparison of the enzyme kinetics for modified versus unmodified enzyme show that modification with camphorquinone-10-sulfonic acid has no effect on the Km for iron but does alter the Km for porphyrin [1].
Treatment with either cyclohexane-1,2-dione or camphorquinone-10-sulfonic acid resulted in between 90 and 98% inhibition of myosin light-chain phosphorylation [2].

Associations of Camphorquinone-10-sulfonic acid with other chemical compounds

Inactivation by 2,3-butanedione, phenylglyoxal and camphorquinone 10-sulfonic acid followed pseudo first-order kinetics with the rate dependent upon modifier concentration [3].

References

The role of arginyl residues in porphyrin binding to ferrochelatase. Dailey, H.A., Fleming, J.E. J. Biol. Chem. (1986) [Pubmed]
Chemical modification of lysine and arginine residues in the myosin regulatory light chain inhibits phosphorylation. Pearson, R.B., Kemp, B.E. Biochim. Biophys. Acta (1986) [Pubmed]
Involvement of arginine residues in glutathione binding to yeast glyoxalase I. Schasteen, C.S., Reed, D.J. Biochim. Biophys. Acta (1983) [Pubmed]

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