The metal requirement of rat tyrosine hydroxylase.
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.
Fitzpatrick
P F
PF
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843.
D000818:Animals; D002384:Catalysis; D004789:Enzyme Activation / Q000187:drug effects; D005296:Ferrous Compounds; D006863:Hydrogen-Ion Concentration; D000644:Quaternary Ammonium Compounds; D051381:Rats; D013379:Substrate Specificity; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism*
D005296:Ferrous Compounds; D000644:Quaternary Ammonium Compounds; C038178:ammonium ferrous sulfate; D014446:Tyrosine 3-Monooxygenase