doi: 10.1016/0167-4838(82)90170-4.
Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens
- PMID: 6809053
- DOI: 10.1016/0167-4838(82)90170-4
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Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens
Biochim Biophys Acta.
.
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.
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