PMID: 6406229Jun 1, 1983Paper

p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 1. Completion of the elucidation of the primary structure

European Journal of Biochemistry
J HofsteengeJ J Beintema

Abstract

As a final step in the elucidation of the primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, the amino acid sequences of a CNBr peptide (CB1, positions 111-276), that accounts for the middle part of the sequence, and the C-terminal CNBr peptide (CB2, positions 277-394) from the enzyme were determined. Important sequence information was obtained from two subfragments that were formed by the cleavage with CNBr of the Met-Thr sequence (positions 346-347) in peptide CB2. The alignment of the two subfragments from peptide CB2 and three one-residue overlaps between peptides from one of these subfragments were confirmed by investigation of well-resolved parts of a 0.25-nm electron-density map. The sequence of residues 343-346 could not be determined with chemical methods and was assigned from the size and shape of the amino acids in the electron-density map. An important tool in the analysis of the amino acid sequence of peptide CB1 was the proteinase Lys-C from Lysobacter enzymogenes, which preferentially cleaves at lysine residues.

References

Jun 15, 1979·Journal of Molecular Biology·R K WierengaJ Drenth
Feb 1, 1978·Analytical Biochemistry·G E TarrD J McKean
Jan 1, 1977·Methods in Enzymology·G E Tarr
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Jan 1, 1963·Acta Chemica Scandinavica·Birger Blomback, Russell F Doolittle

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Citations

Jan 15, 1994·European Journal of Biochemistry·W ZhaoJ Hofsteenge
Jan 12, 1990·European Journal of Biochemistry·T SejlitzH Y Neujahr
Dec 1, 1987·European Journal of Biochemistry·H J Bak, J J Beintema
Jul 1, 1985·FEBS Letters·W Möller, R Amons
Apr 1, 1990·Archives of Biochemistry and Biophysics·S RajasekharanC S Vaidyanathan
Oct 15, 1983·Analytical Biochemistry·P A JekelJ J Beintema
Aug 14, 1992·Biochemical and Biophysical Research Communications·H SumimotoS Minakami

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