The subunit structure of nitrite reductase purified from the denitrifier Achromobacter cycloclastes.
The copper-containing nitrite reductase of Achromobacter cycloclastes has been considered to be a homotrimer with three identical subunits both in the crystal and in solution. In this study, however, the enzyme was found to be a heterotrimer consisting of two subunits with molecular masses of 37 kDa and 36.2 kDa, and the 37 kDa subunit was 6 amino acid residues longer than the smaller subunit. Signal-peptide cleavage sites in its N-terminal region are discussed.
Inatomi
K
K
Advanced Technology R&D Center, Mitsubishi Electric Corp., Hyogo, Japan. inatomi@bio.crl.melco.co.jp
D000421:Alcaligenes / Q000201:enzymology*; D000595:Amino Acid Sequence; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009572:Nitrite Reductases / Q000737:chemistry* / Q000302:isolation & purification; D020836:Protein Structure, Quaternary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D046911:Macromolecular Substances; D009572:Nitrite Reductases