{"title":"草酰乙酸及其结构类似物对柠檬酸裂解酶的失活作用","authors":"Robert Eisenthal, S.S. Tate, S.P. Datta","doi":"10.1016/0926-6593(66)90152-4","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The inactivation of citrate lyase (citrate-oxaloacetate lyase, EC 4.1.3.6) by oxaloacetate has been investigated.</p></span></li><li><span>2.</span><span><p>2. Studies of the pH profiles of inactivation at pH 7–9 with varying total oxaloacetate and magnesium concentrations show that the magnesium complexes of enolic oxaloacetate are involved.</p></span></li><li><span>3.</span><span><p>3. The inhibitory effects of the following structural analogues of the keto and enol forms of oxaloacetate were examined: <span>l</span>-malate, α,α-dimethyloxaloacetate, tartronate, α,α-difluorooxaloacetate, pyruvate, ketomalonate, and isomalate. These results, and the effect of other divalent metal cations, indicate that the site of the inactivation is identical with the active site for citrate cleavage.</p></span></li><li><span>4.</span><span><p>4. The inactivation is irreversible and is time and concentration dependent. Free oxaloacetate does not inactivate the enzyme.</p></span></li><li><span>5.</span><span><p>5. The inactivation phenomenon has high structural specificity, requiring a straight-chain, four-carbon dicarboxylic acid with an ionisable α-hydroxy group, and the presence of a divalent metal cation.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 155-164"},"PeriodicalIF":0.0000,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90152-4","citationCount":"9","resultStr":"{\"title\":\"Inactivation of citrate lyase by oxaloacetate and its structural analogues\",\"authors\":\"Robert Eisenthal, S.S. Tate, S.P. Datta\",\"doi\":\"10.1016/0926-6593(66)90152-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. The inactivation of citrate lyase (citrate-oxaloacetate lyase, EC 4.1.3.6) by oxaloacetate has been investigated.</p></span></li><li><span>2.</span><span><p>2. Studies of the pH profiles of inactivation at pH 7–9 with varying total oxaloacetate and magnesium concentrations show that the magnesium complexes of enolic oxaloacetate are involved.</p></span></li><li><span>3.</span><span><p>3. The inhibitory effects of the following structural analogues of the keto and enol forms of oxaloacetate were examined: <span>l</span>-malate, α,α-dimethyloxaloacetate, tartronate, α,α-difluorooxaloacetate, pyruvate, ketomalonate, and isomalate. These results, and the effect of other divalent metal cations, indicate that the site of the inactivation is identical with the active site for citrate cleavage.</p></span></li><li><span>4.</span><span><p>4. The inactivation is irreversible and is time and concentration dependent. Free oxaloacetate does not inactivate the enzyme.</p></span></li><li><span>5.</span><span><p>5. The inactivation phenomenon has high structural specificity, requiring a straight-chain, four-carbon dicarboxylic acid with an ionisable α-hydroxy group, and the presence of a divalent metal cation.</p></span></li></ul></div>\",\"PeriodicalId\":100160,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"volume\":\"128 1\",\"pages\":\"Pages 155-164\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1966-10-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6593(66)90152-4\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926659366901524\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926659366901524","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Inactivation of citrate lyase by oxaloacetate and its structural analogues
1.
1. The inactivation of citrate lyase (citrate-oxaloacetate lyase, EC 4.1.3.6) by oxaloacetate has been investigated.
2.
2. Studies of the pH profiles of inactivation at pH 7–9 with varying total oxaloacetate and magnesium concentrations show that the magnesium complexes of enolic oxaloacetate are involved.
3.
3. The inhibitory effects of the following structural analogues of the keto and enol forms of oxaloacetate were examined: l-malate, α,α-dimethyloxaloacetate, tartronate, α,α-difluorooxaloacetate, pyruvate, ketomalonate, and isomalate. These results, and the effect of other divalent metal cations, indicate that the site of the inactivation is identical with the active site for citrate cleavage.
4.
4. The inactivation is irreversible and is time and concentration dependent. Free oxaloacetate does not inactivate the enzyme.
5.
5. The inactivation phenomenon has high structural specificity, requiring a straight-chain, four-carbon dicarboxylic acid with an ionisable α-hydroxy group, and the presence of a divalent metal cation.
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