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Nitrite reductase from Pseudomonas aeruginosa : Sequence of the gene and the protein
Author(s) -
Silvestrini Maria Chiara,
Galeotti Cesira L.,
Gervais Michel,
Schininà Eugenia,
Barra Donatella,
Bossa Francesco,
Brunori Maurizio
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81004-x
Subject(s) - periplasmic space , biochemistry , nitrite reductase , amino acid , peptide sequence , signal peptide , chemistry , biology , heme , molecular mass , transmembrane domain , sequence alignment , protein sequencing , gene , enzyme , escherichia coli , nitrate reductase
The gene coding for nitrite reductase of Pseudomonas aeruginosa has been cloned and its sequence determined. The coding region is 1707 bp long and contains information for a polypeptide chain of 568 amino acids. The sequence of the mature protein has been confirmed independently by extensive amino acid sequencing. The amino‐terminus of the mature protein is located at Lys‐26; the preceding 25 residue long extension shows the features typical of signal peptides. Therefore the enzyme is probably secreted into the periplasmic space. The mature protein is made of 543 amino acid residues and has a molecular mass of 60204 Da. The c ‐heme‐binding domain, which contains the only two Cys of the molecule, is located at the amino‐terminal region. Analysis of the protein sequence in terms of hydrophobicity profile gives results consistent with the fact that the enzyme is fully water soluble and not membrane bound; the most hydrophilic region appears to correspond to the c ‐heme domain. Secondary structure predictions are in general agreement with previous analysis of circular dichroic data.