{"title":"乙酰羟基酸合成酶抑制剂:n -邻苯酞- l-缬氨酸苯胺及相关化合物。","authors":"J L Huppatz, J E Casida","doi":"10.1515/znc-1985-9-1010","DOIUrl":null,"url":null,"abstract":"<p><p>The potency of L-valine as an inhibitor of Zea mays acetohydroxyacid synthase (AHAS) is increased more than 8000-fold on conversion to its N-phthalyl anilide derivative which is active at 2 microM. The D-valine, alpha-aminobutyric acid, isoleucine and phenylalanine analogs are 11- to 43-fold less potent, and similar N-phthalyl anilide derivatives of other branched-chain amino acids are essentially inactive. Full potency is retained on replacing the phthalimide moiety of the valine anilide with cyclohexane-1,2-dicarboximide or 1-cyclohexene-1,2-dicarboximide groups and partial activity with 4-cyclohexene-1,2-dicarboximide and methyl- or dimethylmaleimide groups. Inhibition of the enzyme and of root growth by the valine derivatives may result from binding at or near the site involved in feedback control of AHAS by L-valine.</p>","PeriodicalId":23914,"journal":{"name":"Zeitschrift fur Naturforschung. Section C, Biosciences","volume":"40 9-10","pages":"652-6"},"PeriodicalIF":0.0000,"publicationDate":"1985-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znc-1985-9-1010","citationCount":"11","resultStr":"{\"title\":\"Acetohydroxyacid synthase inhibitors: N-phthalyl-L-valine anilide and related compounds.\",\"authors\":\"J L Huppatz, J E Casida\",\"doi\":\"10.1515/znc-1985-9-1010\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The potency of L-valine as an inhibitor of Zea mays acetohydroxyacid synthase (AHAS) is increased more than 8000-fold on conversion to its N-phthalyl anilide derivative which is active at 2 microM. The D-valine, alpha-aminobutyric acid, isoleucine and phenylalanine analogs are 11- to 43-fold less potent, and similar N-phthalyl anilide derivatives of other branched-chain amino acids are essentially inactive. Full potency is retained on replacing the phthalimide moiety of the valine anilide with cyclohexane-1,2-dicarboximide or 1-cyclohexene-1,2-dicarboximide groups and partial activity with 4-cyclohexene-1,2-dicarboximide and methyl- or dimethylmaleimide groups. Inhibition of the enzyme and of root growth by the valine derivatives may result from binding at or near the site involved in feedback control of AHAS by L-valine.</p>\",\"PeriodicalId\":23914,\"journal\":{\"name\":\"Zeitschrift fur Naturforschung. Section C, Biosciences\",\"volume\":\"40 9-10\",\"pages\":\"652-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1985-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/znc-1985-9-1010\",\"citationCount\":\"11\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift fur Naturforschung. Section C, Biosciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/znc-1985-9-1010\",\"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-1985-9-1010","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 11
摘要
l -缬氨酸作为玉米乙酰羟基酸合成酶(AHAS)抑制剂,转化为其n -邻苯乙基苯胺衍生物后,其活性在2微米时增加了8000倍以上。d-缬氨酸、α -氨基丁酸、异亮氨酸和苯丙氨酸类似物的效力要低11- 43倍,其他支链氨基酸的类似n -苯乙基苯胺衍生物基本上没有活性。用环己烷-1,2-二碳酰亚胺或1-环己烷-1,2-二碳酰亚胺取代缬氨酸苯胺的邻苯二亚胺部分,部分活性用4-环己烷-1,2-二碳酰亚胺和甲基或二甲基马来酰亚胺取代时,效力保持完整。缬氨酸衍生物对酶和根生长的抑制可能是由于与l -缬氨酸反馈控制AHAS的位点或附近的结合。
Acetohydroxyacid synthase inhibitors: N-phthalyl-L-valine anilide and related compounds.
The potency of L-valine as an inhibitor of Zea mays acetohydroxyacid synthase (AHAS) is increased more than 8000-fold on conversion to its N-phthalyl anilide derivative which is active at 2 microM. The D-valine, alpha-aminobutyric acid, isoleucine and phenylalanine analogs are 11- to 43-fold less potent, and similar N-phthalyl anilide derivatives of other branched-chain amino acids are essentially inactive. Full potency is retained on replacing the phthalimide moiety of the valine anilide with cyclohexane-1,2-dicarboximide or 1-cyclohexene-1,2-dicarboximide groups and partial activity with 4-cyclohexene-1,2-dicarboximide and methyl- or dimethylmaleimide groups. Inhibition of the enzyme and of root growth by the valine derivatives may result from binding at or near the site involved in feedback control of AHAS by L-valine.