破坏性氧对苯丙氨酸羟化酶失活可能机制的研究。

R M Fink, E F Elstner
{"title":"破坏性氧对苯丙氨酸羟化酶失活可能机制的研究。","authors":"R M Fink,&nbsp;E F Elstner","doi":"10.1515/znc-1984-7-809","DOIUrl":null,"url":null,"abstract":"<p><p>The enzymic hydroxylation of phenylalanine by phenylalanine hydroxylase (E.C. 1.14.16.1.) in vitro is dependent on the presence of hydrogen peroxide removing processes. The loss of phenylalanine hydroxylase activity can be prevented to the same extent by catalase as well as the presence of optimized amounts of both peroxidase and superoxide dismutase. Peroxidase alone exhibited only two third of the maximal protective effect of catalase whereas superoxide dismutase alone was not able to exert any protective influence on phenylalanine hydroxylase. These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.</p>","PeriodicalId":23914,"journal":{"name":"Zeitschrift fur Naturforschung. Section C, Biosciences","volume":"39 7-8","pages":"734-7"},"PeriodicalIF":0.0000,"publicationDate":"1984-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znc-1984-7-809","citationCount":"5","resultStr":"{\"title\":\"Studies on the possible mechanism of inactivation of phenylalanine hydroxylase by destructive oxygen species.\",\"authors\":\"R M Fink,&nbsp;E F Elstner\",\"doi\":\"10.1515/znc-1984-7-809\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The enzymic hydroxylation of phenylalanine by phenylalanine hydroxylase (E.C. 1.14.16.1.) in vitro is dependent on the presence of hydrogen peroxide removing processes. The loss of phenylalanine hydroxylase activity can be prevented to the same extent by catalase as well as the presence of optimized amounts of both peroxidase and superoxide dismutase. Peroxidase alone exhibited only two third of the maximal protective effect of catalase whereas superoxide dismutase alone was not able to exert any protective influence on phenylalanine hydroxylase. These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.</p>\",\"PeriodicalId\":23914,\"journal\":{\"name\":\"Zeitschrift fur Naturforschung. Section C, Biosciences\",\"volume\":\"39 7-8\",\"pages\":\"734-7\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1984-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/znc-1984-7-809\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift fur Naturforschung. Section C, Biosciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/znc-1984-7-809\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zeitschrift fur Naturforschung. Section C, Biosciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/znc-1984-7-809","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5

摘要

在体外,苯丙氨酸羟化酶(E.C. 1.14.16.1.)对苯丙氨酸的酶羟基化作用依赖于过氧化氢去除过程的存在。苯丙氨酸羟化酶活性的丧失可以通过过氧化氢酶以及优化量的过氧化物酶和超氧化物歧化酶的存在来防止。单独的过氧化物酶仅表现出过氧化氢酶最大保护作用的三分之二,而单独的超氧化物歧化酶不能对苯丙氨酸羟化酶产生任何保护作用。这些发现表明,在没有过氧化氢去除反应的情况下,苯丙氨酸羟化的终止可能是由于在H2O2和四氢蝶呤辅助因子存在下,苯丙氨酸羟化酶的活性位点铁产生了破坏性的氧。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Studies on the possible mechanism of inactivation of phenylalanine hydroxylase by destructive oxygen species.

The enzymic hydroxylation of phenylalanine by phenylalanine hydroxylase (E.C. 1.14.16.1.) in vitro is dependent on the presence of hydrogen peroxide removing processes. The loss of phenylalanine hydroxylase activity can be prevented to the same extent by catalase as well as the presence of optimized amounts of both peroxidase and superoxide dismutase. Peroxidase alone exhibited only two third of the maximal protective effect of catalase whereas superoxide dismutase alone was not able to exert any protective influence on phenylalanine hydroxylase. These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
A disappearance of a 24-kDa acid-soluble protein from liver chromatin of normal and starved hens following D-galactosamine administration. Further observations on periodicities of nucleotide occurrences in natural DNA's. Reaction of fluorescein isothiocyanate with thiol and amino groups of sarcoplasmic ATPase. Formation and decay of the vanadate complex of the sarcoplasmic reticulum calcium transport protein. MTD approach to quantitative structure-activity relationships for cardiotonic steroids.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1