Phenylalanine as substrate for tyrosine hydroxylase in bovine adrenal chromaffin cells

  • Biochem J. 1990 Jun 1;268(2):525-8. doi: 10.1042/bj2680525.
M H Fukami  1 ,  J Haavik ,  T Flatmark
Affiliations
  • 1. Department of Biochemistry, University of Bergen, Norway.
PMID: 1973034 DOI: 10.1042/bj2680525
Abstract

Incubation of bovine chromaffin cells with L-[14C]phenylalanine resulted in label accumulation in catecholamines at about 30% of the rate seen with L-tyrosine as precursor. Studies with purified Tyrosine Hydroxylase (EC 1.14.16.2) showed that the enzyme catalysed the hydroxylation of L-phenylalanine first to L-p-tyrosine and then to 3,4-dihydroxyphenylalanine (DOPA). No evidence for a significant involvement of an L-m-tyrosine intermediate in DOPA formation was found.

Products