Domke I, Weis W
Biochem Biophys Res Commun. 1983 Jul 29;114(2):578-83. doi: 10.1016/0006-291x(83)90819-7.
Alloxan behaves as a substrate for NADH:ferricytochrome b5 oxidoreductase (EC 1.6.2.2). The apparent Km for alloxan was 10 mM in liver microsomes and 20 mM with the enzyme prepared by lysosomal digestion. The apparent Km for NADH was the same with microsomes and the isolated enzyme (30 microM). The maximum turnover rate was calculated as 426 moles electrons/min X mole enzyme. Cytochrome b5 was shown to reduce alloxan nonenzymatically.
四氧嘧啶可作为NADH：铁细胞色素b5氧化还原酶（EC 1.6.2.2）的底物。在肝微粒体中，四氧嘧啶的表观Km为10 mM，而用溶酶体消化制备的酶的表观Km为20 mM。NADH的表观Km在微粒体和分离的酶中相同（30 microM）。最大周转率计算为426摩尔电子/分钟×摩尔酶。细胞色素b5被证明可非酶促还原四氧嘧啶。
