| Literature DB >> 3488060 |
Y Ozaki, J F Reinhard, C A Nichol.
Abstract
Dihydroflavin mononucleotide (FMNH2) and tetrahydrobiopterin (BH4) serve as cofactors for indoleamine 2,3-dioxygenase isolated from mouse epididymis. The optimal pH was between 7 and 8, and FMNH2-dependent activity was 4 to 5-fold higher than activity with methylene blue as the electron donor. Using FMNH2 with a FMN reductase system, the enzyme exhibited higher efficiency and specificity for L-Trp (an apparent Km of 1 X 10(-5)M and an apparent Vmax of 182 nmol/min/mg of protein). The apparent Km and Vmax for D-Trp were 6.2 X 10(-5)M and 31 nmole/min/mg, respectively. Consequently, these observations appear to present the first evidence for a flavin-dependent mammalian dioxygenase.Entities:
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Year: 1986 PMID： 3488060 DOI： 10.1016/0006-291x(86)90339-6
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575