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PMID: 6809053 Published · ppublish English Journal Article

Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.

Biochimica et biophysica acta ·Vol. 704 ·No. 2 ·1982-06-04 ·Pages 385-8

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

Abstract

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.

MeSH Terms
4-Hydroxybenzoate-3-Monooxygenase Amino Acid Sequence Mixed Function Oxygenases Pseudomonas fluorescens/enzymology
Chemicals
Mixed Function Oxygenases 4-Hydroxybenzoate-3-Monooxygenase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Weijer W J
Hofsteenge J
Vereijken J M
Jekel P A
Beintema J J
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1982-06-04
Pages
385-8
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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