A NEW REDOX COFACTOR IN EUKARYOTIC ENZYMES - 6-HYDROXYDOPA AT THE ACTIVE-SITE OF BOVINE SERUM AMINE OXIDASE
A NEW REDOX COFACTOR IN EUKARYOTIC ENZYMES - 6-HYDROXYDOPA AT THE ACTIVE-SITE OF BOVINE SERUM AMINE OXIDASE
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DOI：
10.1126/science.2111581
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发表时间：
1990-05-25
期刊：
影响因子：
56.9
通讯作者：
KLINMAN, JP
中科院分区：
文献类型：
--
作者：
JANES, SM;MU, D;KLINMAN, JP
从牛血清胺氧化酶中高产得一种活性位点、含辅助因子的肽。该五肽的序列为：Leu-Asn-X-Sp-Tyr。通过质谱分析、紫外可见光谱分析和质子核磁共振分析，X被鉴定为6-氢多巴。这一结果表明，与以往的建议相反，吡咯喹啉醌不是哺乳动物铜胺氧化酶的活性位点辅助因子。虽然6-羟多巴与神经毒性有关，但目前的数据表明，该化合物在酶活性位点具有功能作用。
An active site, cofactor-containing peptide has been obtained in high yield from bovine serum amine oxidase. Sequencing of this pentapeptide indicates: Leu-Asn-X-Sp-Tyr. Analysis of the peptide by mass spectrometry, ultraviolet-visible spectroscopy, and proton nuclear magnetic resonance leads to the identification of X as 6-hydrodopa. This result indicates that, contrary to previous proposals, pyrroloquinoline quinone is not the active site cofactor in mammalian copper amine oxidases. Although 6-hydroxydopa has been implicated in neurotoxicity, the data presented suggest that this compound has a functional role at an enzyme active site.