rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1997-3-6
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pubmed:databankReference |
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pubmed:abstractText |
To discover the molecular properties of two distinct NADH oxidases, corresponding to H2O2-forming oxidase (NOX-1) and H2O-forming oxidase (NOX-2) induced in Streptococcus mutans, for the first step we had cloned and sequenced the nox-1 gene encoding NOX-1. In this paper, a nox-2 gene encoding NOX-2 from S. mutans was cloned, and the nucleotides sequenced. The nox-2 gene comprises 1371 base-pairs, encoding a polypeptide of 457 amino acid residues. The deduced relative molecular mass (M(r) = 49919) agreed with the previous value obtained from the purified NOX-2 protein. The nox-2 gene was expressed in Escherichia coli using its own promoter. Alignment of the NOX-2 protein sequence with that of the NOX-1 showed that the proteins do not significantly resemble each other. Comparisons with the NADH oxidase from Streptococcus faecalis 10C1 yield identities of 41%. The redox-active cysteine in the enzyme from S. faecalis was found to correspond to Cys 44 in the NOX-2.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
B
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Jan
|
pubmed:issn |
0916-8451
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39-43
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8824824-Amino Acid Sequence,
pubmed-meshheading:8824824-Blotting, Western,
pubmed-meshheading:8824824-Cloning, Molecular,
pubmed-meshheading:8824824-Cysteine,
pubmed-meshheading:8824824-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8824824-Enterococcus faecalis,
pubmed-meshheading:8824824-Escherichia coli,
pubmed-meshheading:8824824-Gene Expression Regulation, Bacterial,
pubmed-meshheading:8824824-Molecular Sequence Data,
pubmed-meshheading:8824824-Molecular Weight,
pubmed-meshheading:8824824-Multienzyme Complexes,
pubmed-meshheading:8824824-NADH, NADPH Oxidoreductases,
pubmed-meshheading:8824824-Oxidation-Reduction,
pubmed-meshheading:8824824-Promoter Regions, Genetic,
pubmed-meshheading:8824824-Sequence Alignment,
pubmed-meshheading:8824824-Sequence Homology, Amino Acid,
pubmed-meshheading:8824824-Streptococcus mutans,
pubmed-meshheading:8824824-Water
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pubmed:year |
1996
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pubmed:articleTitle |
Molecular cloning and sequence analysis of the gene encoding the H2O-forming NADH oxidase from Streptococcus mutans.
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pubmed:affiliation |
Research Center, Nippon Paint Co., Ltd., Osaka, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study
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