Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding

Arch Biochem Biophys. 1999 Jul 1;367(1):143-5. doi: 10.1006/abbi.1999.1259.
No abstract available

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites / drug effects
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Cyclic AMP-Dependent Protein Kinases / pharmacology
  • Dopamine / metabolism*
  • Kinetics
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Phosphorylation / drug effects
  • Phosphoserine / metabolism
  • Protein Binding
  • Protein Conformation / drug effects
  • Rats
  • Structure-Activity Relationship
  • Trypsin / metabolism*
  • Tyrosine 3-Monooxygenase / chemistry
  • Tyrosine 3-Monooxygenase / metabolism*

Substances

  • Peptide Fragments
  • Phosphoserine
  • Tyrosine 3-Monooxygenase
  • Cyclic AMP-Dependent Protein Kinases
  • Trypsin
  • Dopamine