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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Ozaki Y,Reinhard JF Jr,Nichol CAdoi
10.1016/0006-291x(86)90339-6subject
Has Abstractpub_date
1986-06-30 00:00:00pages
1106-11issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(86)90339-6journal_volume
137pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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pub_type: 杂志文章
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journal_title:Biochemical and biophysical research communications
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