Reduction of mitomycin C is catalysed by human recombinant NRH:quinone oxidoreductase 2 using reduced nicotinamide adenine dinucleotide as an electron donating co-factor.
Br J Cancer
; 95(9): 1229-33, 2006 Nov 06.
Article
in En
| MEDLINE
| ID: mdl-17031400
ABSTRACT
NRHQuinone Oxidoreductase 2 (NQO2) has been described as having no enzymatic activity with nicotinamide adenine dinucleotide (NADH) or NADPH as electron donating cosubstrates. Mitomycin C (MMC) is both a substrate for and a mechanistic inhibitor of the NQO2 homologue NQO1. NRHquinone oxidoreductase 2 catalysed the reduction of MMC at pH 5.8 with NADH as a co-factor. This reaction results in species that inhibit the NQO2-mediated metabolism of CB1954. In addition, MMC caused an increase in DNA cross-links in a cell line transfected to overexpress NQO2 to an extent comparable to that observed with an isogenic NQO1-expressing cell line. These data indicate that NQO2 may contribute to the metabolism of MMC to cytotoxic species.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Quinone Reductases
/
Mitomycin
/
NAD
Limits:
Animals
/
Humans
Language:
En
Journal:
Br J Cancer
Year:
2006
Document type:
Article
Affiliation country: