2. Academic Validation
  3. Phenylalanine as substrate for tyrosine hydroxylase in bovine adrenal chromaffin cells

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

Affiliation

  • 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.

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