The metal requirement of rat tyrosine hydroxylase

Biochem Biophys Res Commun. 1989 May 30;161(1):211-5. doi: 10.1016/0006-291x(89)91582-9.

Abstract

The effect of added metals on purified rat tyrosine hydroxylase which is predominantly iron-free has been determined. The presence of 10 microM ferrous ammonium sulfate results in a ten-fold increase in the activity of enzyme containing 0.1 iron atom per subunit. The enzyme activity is half-maximal at a free ferrous iron concentration of 0.15 microM. Copper, zinc, silver, and nickel are unable to replace ferrous iron. Ferric iron is inactive unless ascorbate is included to reduce it.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Catalysis
  • Enzyme Activation / drug effects
  • Ferrous Compounds*
  • Hydrogen-Ion Concentration
  • Quaternary Ammonium Compounds*
  • Rats
  • Substrate Specificity
  • Tyrosine 3-Monooxygenase / metabolism*

Substances

  • Ferrous Compounds
  • Quaternary Ammonium Compounds
  • ammonium ferrous sulfate
  • Tyrosine 3-Monooxygenase