6-pyruvoyl tetrahydropterin synthase from salmon liver: amino acid sequence analysis by tandem mass spectrometry.

Abstract

The most frequent variant of atypical phenylketonuria, an inborn error of metabolism, is characterized by a low activity of the 6-pyruvoyl tetrahydropterin synthase. We purified and characterized this enzyme from salmon liver known to contain high levels. After digestion, peptides were sequenced by tandem mass spectrometry and/or automated Edman microsequence analysis. Both a free amine terminus and an N-acetylated amine terminus were found, indicating the presence of two isoforms. The peptide sequences determined here have a high degree of homology with the protein sequence deduced from cDNA for rat 6-pyruvoyl tetrahydropterin synthase (1), however, the amine termini of these proteins differ significantly.

• Authors: C R Hauer, W Leimbacher, P Hunziker, F Neuheiser, N Blau, C W Heizmann
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 182 Issue 2 Pg. 953-9 (Jan 31 1992) ISSN: 0006-291X [Print] United States
• PMID: 1734893 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Indicators and Reagents
• Peptide Fragments
• Alcohol Oxidoreductases
• Phosphorus-Oxygen Lyases
• 6-pyruvoyltetrahydropterin synthase

Topics

• Alcohol Oxidoreductases (chemistry, genetics, isolation & purification)
• Amino Acid Sequence
• Animals
• Chromatography, High Pressure Liquid
• Electrophoresis, Gel, Two-Dimensional
• Electrophoresis, Polyacrylamide Gel
• Indicators and Reagents
• Liver (enzymology)
• Mass Spectrometry
• Molecular Sequence Data
• Molecular Weight
• Peptide Fragments (isolation & purification)
• Phosphorus-Oxygen Lyases
• Rats
• Salmon
• Sequence Homology, Nucleic Acid