Primary structure of p-hydroxybenzoate hydroxylase...[Biochim Biophys Acta. 1982]

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1: Biochim Biophys Acta. 1982 Jun 4;704(2):385-8. Links

Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.

Weijer WJ, Hofsteenge J, Vereijken JM, Jekel PA, Beintema JJ.

The amino acid sequence of the p-hydroxybenzoate hydroxylase (4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating), EC 1.14.13.2) monomer from Pseudomonas fluorescens has been determined. The sequence was elucidated by a combination of the results from an X-ray crystallographic study at 0.25 nm resolution (Wierenga, R.K., de Jong, R.J., Kalk, K.H., Hol, W.G.J. and Drenth, J. (1979) J. Mol. Biol. 131, 55-73) and from protein sequence analysis. The polypeptide chain of the monomer contains 394 amino acids and has a molecular weight of 44 299.

PMID: 6809053 [PubMed - indexed for MEDLINE]

Primary and tertiary structure studies of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Isolation and alignment of the CNBr peptides; interactions of the protein with flavin adenine dinucleotide.
Eur J Biochem. 1980 Dec; 113(1):141-50.

[Eur J Biochem. 1980]
p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure.
Eur J Biochem. 1983 Jun 1; 133(1):109-18.

[Eur J Biochem. 1983]
The amino-acid sequence of the three smallest CNBr peptides from p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
Eur J Biochem. 1980 Dec; 113(1):151-7.

[Eur J Biochem. 1980]
ReviewProtein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.
Arch Biochem Biophys. 2005 Jan 1; 433(1):297-311.

[Arch Biochem Biophys. 2005]
ReviewStructure and mechanism of para-hydroxybenzoate hydroxylase.
FASEB J. 1995 Apr; 9(7):476-83.

[FASEB J. 1995]
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[Appl Environ Microbiol. 1997]
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