Update on interconversions of vitamin B-6 with its coenzyme.
Update on interconversions of vitamin B-6 with its coenzyme.
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DOI：
10.1093/jn/129.2.325
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发表时间：
1999-02
期刊：
影响因子：
--
通讯作者：
D. B. Mccormick;Haoyuan Chen
中科院分区：
文献类型：
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作者：
D. B. Mccormick;Haoyuan Chen
吡哆醛5 '-磷酸（PLP）的生物合成依赖于两种连续酶的相对特异性作用，即吡哆醛（吡哆醇、吡哆胺）激酶和吡哆醇（吡哆胺）磷酸氧化酶。不太特异的磷酸酶催化维生素吡哆醛、吡哆胺和吡哆醇的5 '-磷酸的水解。从一代人以前认识到三种形式的维生素B-6及其5 '-磷酸盐相互转化的这些过程开始，最近的研究提供了对所涉及的酶的分子特征的相当复杂的理解。吡哆醛激酶的同源部分在人类以及细菌中的进化保留，以及最近发现的吡哆醇（吡哆胺）磷酸氧化酶的高度保守区域，也来自原核生物和真核生物，强调了这些催化剂在大多数生物体所必需的辅酶形成中的重要性。参与B-6代谢的激酶和氧化酶都是药物的潜在靶点。
Biosynthesis of pyridoxal 5'-phosphate (PLP) depends upon the relatively specific action of two consecutive enzymes, viz. pyridoxal (pyridoxine, pyridoxamine) kinase and pyridoxine (pyridoxamine) phosphate oxidase. Less specific phosphatases catalyze hydrolyses of the 5'-phosphates of the vitamers pyridoxal, pyridoxamine, and pyridoxine. From the recognition a generation ago of these processes by which the three forms of vitamin B-6 and their 5'-phosphates are interconverted, more recent studies have provided a fairly sophisticated understanding of the molecular characteristics of the enzymes involved. The evolutionary retention of homologous portions of pyridoxal kinase in humans as well as bacteria and the most recent finding of a highly conserved region of the pyridoxine (pyridoxamine) phosphate oxidase, also from both prokaryotic and eukaryotic organisms, emphasize the importance of these catalysts in the formation of a coenzyme that is essential for most organisms. Both kinase and oxidase involved in B-6 metabolism are potential targets for pharmacologic agents.