{"title":"Allantoinases from bacterial, plant and animal sources I. Purification and enzymic properties","authors":"G.D. Vogels, F. Trijbels, A. Uffink","doi":"10.1016/0926-6593(66)90040-3","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Allantoinases (allantoin amidohydrolase, EC 3.5.2.5) from <em>Streptococcus allantoicus, Arthrobacter allantoicus, Escherichia coli, Pseudomonas fluorescens, Pseudomonas acidovorans</em>, frog liver, goldfish liver, <em>Phaseolus hysterinus</em> and <em>Glycine hispida</em> were studied.</p></span></li><li><span>2.</span><span><p>2. The enzymes were purified 2.5- to 37-fold by (NH<sub>4</sub>)<sub>2</sub>SO<sub>4</sub> precipitation and DEAE-cellulose chromatography.</p></span></li><li><span>3.</span><span><p>3. The pH optimum curve, Michaelis constant, activation energy, stability and specificity were determined and compared.</p></span></li><li><span>4.</span><span><p>4. The enzymes from <em>S. allantoicus, A. allantoicus</em> and <em>E. coli</em> were aspecific; the others degraded (+)-allantoin 4–22 times faster than (−)-allantoin.</p></span></li><li><span>5.</span><span><p>5. The allantoinases from <em>Ph. hysterinus</em> and <em>G. hispida</em> were activated by acid pretreatment below pH 5.4.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1966-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90040-3","citationCount":"46","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/0926659366900403","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 46
Abstract
1.
1. Allantoinases (allantoin amidohydrolase, EC 3.5.2.5) from Streptococcus allantoicus, Arthrobacter allantoicus, Escherichia coli, Pseudomonas fluorescens, Pseudomonas acidovorans, frog liver, goldfish liver, Phaseolus hysterinus and Glycine hispida were studied.
2.
2. The enzymes were purified 2.5- to 37-fold by (NH4)2SO4 precipitation and DEAE-cellulose chromatography.
3.
3. The pH optimum curve, Michaelis constant, activation energy, stability and specificity were determined and compared.
4.
4. The enzymes from S. allantoicus, A. allantoicus and E. coli were aspecific; the others degraded (+)-allantoin 4–22 times faster than (−)-allantoin.
5.
5. The allantoinases from Ph. hysterinus and G. hispida were activated by acid pretreatment below pH 5.4.