کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1926703 | 1536467 | 2008 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Biochemical characterization of l-DOPA 2,3-dioxygenase, a single-domain type I extradiol dioxygenase from lincomycin biosynthesis Biochemical characterization of l-DOPA 2,3-dioxygenase, a single-domain type I extradiol dioxygenase from lincomycin biosynthesis](/preview/png/1926703.png)
l-DOPA-2,3-dioxygenase from Streptomyces lincolnensis is a single-domain type I extradiol dioxygenase of the vicinal oxygen chelate superfamily and catalyzes the second step in the metabolism of tyrosine to the propylhygric acid moiety of the antibiotic, lincomycin. S. lincolnensisl-DOPA-2,3-dioxygenase was overexpressed, purified and reconstituted with Fe(II). The activity of l-DOPA-2,3-dioxygenase was kinetically characterized with l-DOPA (KM = 38 μM, kcat = 4.2 min−1) and additional catecholic substrates including dopamine, 3,4-dihydroxyhydrocinnamic acid, catechol and d-DOPA. 3,4-Dihydroxyphenylacetic acid was characterized as a competitive inhibitor of the enzyme (Ki = 2.2 mM). Site-directed mutagenesis and its effects on enzymatic activity were used to identify His14 and His70 as iron ligands.
Journal: Archives of Biochemistry and Biophysics - Volume 479, Issue 2, 15 November 2008, Pages 131–138