The N-terminal amino acid sequence of phenol hydroxylase contains a dinucleotide-binding sequence motif.
The N-terminal sequence of phenol hydroxylase from Trichosporon cutaneum was determined by Edman degradation of the integral protein and of fragments obtained by hydroxylamine cleavage and by digestion with Staphylococcus V8 protease. A continuous sequence of 80 residues from the N terminus was determined: TKYSESYCDV10, LIVGAGPAGL20 MAARVLSEYV30 RQKPDLKVRI40 IDKRSTKVYN50 GQADGLQCRT60 LESLKNLRLA70 DKIXSEXNDM80. A single N-terminal sequence was detected, suggesting two identical subunits in the dimeric enzyme. We suggest the occurrence of an FAD-binding site near the N terminus. The C-terminal sequence is -LSTA, as determined by carboxypeptidase digestion.
Department of Biochemistry and Biotechnology, Royal Institute of Technology, Stockholm, Sweden.
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Sejlitz
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Wernstedt
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D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D002373:Cyclic AMP Receptor Protein; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D006868:Hydrolysis; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D012697:Serine Endopeptidases; D014250:Trichosporon / Q000201:enzymology
D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D005656:Fungal Proteins; D010446:Peptide Fragments; D005182:Flavin-Adenine Dinucleotide; D006899:Mixed Function Oxygenases; C022336:phenol 2-monooxygenase; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase