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大鼠肝脏中植烷酸的α氧化:α羟基化研究

Phytanic acid alpha oxidation in rat liver: studies on alpha hydroxylation.

作者信息

Muralidharan F N, Muralidharan V B

出版信息

Int J Biochem. 1987;19(8):663-70. doi: 10.1016/0020-711x(87)90078-4.

DOI:10.1016/0020-711x(87)90078-4
PMID:3622898
Abstract
  1. The alpha-hydroxylation of [1-14C]phytanic acid was investigated in the postnuclear fraction of rat liver. 2. The reaction required ATP, Mg, Fe3+ and molecular oxygen. Fe3+ could be replaced by Fe2+. 3. The hydroxylase activity was optimal at pH 7.5 in phosphate buffer. 4. The activity increased with postnuclear protein (5-13 mg or protein), increased with the substrate concentration at low substrate concentration. 5. The amount of the hydroxyacid formed increased with time up to 10 min. 6. Coenzyme A (100 microM-2.5 mM) stimulated the activity. 7. The activity was further stimulated by NADP and NADPH slightly and by FAD and FMN strongly, all at 100 microM concentration. 8. While CO inhibited the reaction, phenobarbital inducible cytochrome P-450 did not appear to play a role in this reaction.
摘要
  1. 研究了[1-14C]植烷酸在大鼠肝脏核后组分中的α-羟基化作用。2. 该反应需要ATP、Mg、Fe3+和分子氧。Fe3+可用Fe2+替代。3. 羟化酶活性在磷酸盐缓冲液中pH 7.5时最佳。4. 活性随核后蛋白(5-13毫克蛋白)增加,在低底物浓度时随底物浓度增加。5. 形成的羟基酸量随时间增加,直至10分钟。6. 辅酶A(100微摩尔-2.5毫摩尔)刺激该活性。7. 在100微摩尔浓度下,NADP和NADPH对活性有轻微刺激作用,FAD和FMN对活性有强烈刺激作用。8. 虽然CO抑制该反应,但苯巴比妥诱导的细胞色素P-450似乎在该反应中不起作用。

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Phytanic acid alpha oxidation in rat liver: studies on alpha hydroxylation.大鼠肝脏中植烷酸的α氧化:α羟基化研究
Int J Biochem. 1987;19(8):663-70. doi: 10.1016/0020-711x(87)90078-4.
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Phytanic acid alpha-oxidation in rat liver. Requirement of cytosolic factor.大鼠肝脏中植烷酸的α-氧化。胞质因子的需求。
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Evidence against alpha-hydroxyphytanic acid as an intermediate in the metabolism of phytanic acid.反对α-羟基植烷酸作为植烷酸代谢中间体的证据。
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Characterization of phytol-phytanate conversion activity in rat liver.
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The subcellular localization of phytanic acid oxidase in rat liver.植烷酸氧化酶在大鼠肝脏中的亚细胞定位。
Biochim Biophys Acta. 1987 Sep 4;921(1):38-42. doi: 10.1016/0005-2760(87)90167-6.
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Eur J Biochem. 1987 Sep 15;167(3):573-8. doi: 10.1111/j.1432-1033.1987.tb13374.x.
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