Primary amino acid sequence of bovine dopamine β-hydroxylase

James G. Robertson, Parimal R. Desai, Alok Kumar, G. King Farrington, Paul F Fitzpatrick, Joseph J. Villafranca

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Fifty-eight tryptic and Staphylococcus aureus V8 protease generated peptides from bovine dopamine β-hydroxylase were isolated by reverse-phase high pressure liquid chromatography and sequenced. These peptide sequences were compared with the deduced amino acid sequences of bovine and human dopamine β-hydroxylase obtained from the cloned cDNAs. Bovine peptide sequences had five differences with the sequence derived from the bovine cDNA, and four of the changes could be accounted for by a single base change in the DNA. N-terminal sequence analysis of the bovine enzyme indicated that it contained two N termini, one of which is 3 amino acids longer than the other and begins with the sequence Ser-Ala-Pro. The amino acid sequences deduced from the bovine and human cDNAs are 19 and 25 amino acids longer, respectively, and these additional amino acids represent leader peptide sequences. Two bovine peptide sequences contained glycosylation sites and gave positive tests for carbohydrate residues, and two others contained the consensus sequence for a glycosylation site but were negative in the carbohydrate test. The bovine enzyme contains 6 Trp, as compared with 7 in the bovine cDNA and 8 in the human cDNA. The protein and bovine cDNA contain 24 Tyr each, as compared with 26 in the human cDNA. These numbers indicate that the true ε280 1%= 8.95, and, therefore, that it is 28% lower than the previously determined value. The data also identify 5 His-containing regions that may be involved in Cu2+ coordination at the active site.

Original languageEnglish (US)
Pages (from-to)1029-1035
Number of pages7
JournalJournal of Biological Chemistry
Volume265
Issue number2
StatePublished - Jan 15 1990
Externally publishedYes

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Mixed Function Oxygenases
Amino Acid Sequence
Dopamine
Complementary DNA
Amino Acids
Glycosylation
Peptides
Carbohydrates
High pressure liquid chromatography
Enzymes
Protein Sorting Signals
Consensus Sequence
Reverse-Phase Chromatography
Sequence Analysis
Staphylococcus aureus
Catalytic Domain
DNA
High Pressure Liquid Chromatography
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Robertson, J. G., Desai, P. R., Kumar, A., Farrington, G. K., Fitzpatrick, P. F., & Villafranca, J. J. (1990). Primary amino acid sequence of bovine dopamine β-hydroxylase. Journal of Biological Chemistry, 265(2), 1029-1035.

Primary amino acid sequence of bovine dopamine β-hydroxylase. / Robertson, James G.; Desai, Parimal R.; Kumar, Alok; Farrington, G. King; Fitzpatrick, Paul F; Villafranca, Joseph J.

In: Journal of Biological Chemistry, Vol. 265, No. 2, 15.01.1990, p. 1029-1035.

Research output: Contribution to journalArticle

Robertson, JG, Desai, PR, Kumar, A, Farrington, GK, Fitzpatrick, PF & Villafranca, JJ 1990, 'Primary amino acid sequence of bovine dopamine β-hydroxylase', Journal of Biological Chemistry, vol. 265, no. 2, pp. 1029-1035.
Robertson JG, Desai PR, Kumar A, Farrington GK, Fitzpatrick PF, Villafranca JJ. Primary amino acid sequence of bovine dopamine β-hydroxylase. Journal of Biological Chemistry. 1990 Jan 15;265(2):1029-1035.
Robertson, James G. ; Desai, Parimal R. ; Kumar, Alok ; Farrington, G. King ; Fitzpatrick, Paul F ; Villafranca, Joseph J. / Primary amino acid sequence of bovine dopamine β-hydroxylase. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 2. pp. 1029-1035.
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