Molecular cloning and sequence analysis of the gene encoding the H2O2-forming NADH oxidase from Streptococcus mutans

Higuchi, M.; Shimada, M.; Matsumoto, J.; Yamamoto, Y.; Rhaman, A.; Kamio, Y.

Bioscience Biotechnology and Biochemistry 58(9): 1603-1607


ISSN/ISBN: 0916-8451
PMID: 7765479
DOI: 10.1271/bbb.58.1603
Accession: 059983331

Download citation:  

Article/Abstract emailed within 0-6 h
Payments are secure & encrypted
Powered by Stripe
Powered by PayPal

Streptococcus mutans induces both H2O2-forming and H2O-forming NADH oxidases in the presence of O2 [M. Higuchi, J. Gen. Microbiol., 130, 1819-1826 (1984)]. In this paper, a nox-1 gene encoding H2O2-forming NADH oxidase (NOX-1) from Streptococcus mutans was cloned, and the nucleotides sequenced. The structural gene of nox-1 consisted of 1530 base pairs, which encode a polypeptide consisting of 510 amino acids with a predicted molecular mass of 55,196 Da. The deduced N-terminal amino acid sequence was consistent with that previously found for the purified NOX-1 protein. The nox-1 gene was expressed in Escherichia coli using its own promoter. Alignment of the amino acid sequence of NOX-1 with those of NADH oxidases from other microorganisms showed identities of 55.6%, 20.8%, 20.3%, and 7.3% for those of Amphibacillus xylanus Ep01, Streptococcus faecalis 10C1, Thermoanaerobium brockii Rt8.G4, and Thermus thermophilus HB8, respectively.