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dc.contributor.authorChen, Q. X.zh_CN
dc.contributor.authorLu, H. Y.zh_CN
dc.contributor.authorZhu, C. M.zh_CN
dc.contributor.authorLin, H. N.zh_CN
dc.contributor.authorZhou, H. M.zh_CN
dc.contributor.author陈清西zh_CN
dc.date.accessioned2013-12-12T02:24:34Z
dc.date.available2013-12-12T02:24:34Z
dc.date.issued1998-07zh_CN
dc.identifier.citationBiochemistry and Molecular Biology International, 1998,45(3):465-473zh_CN
dc.identifier.issn1039-9712zh_CN
dc.identifier.otherISI:000074892100005zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65646
dc.description.abstractGreen crab (Scylla Serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme which catalyzed the nonspecific hydrolysis of phosphate monoesters. In the present paper, the effects of several N-thiophosphoryl amino acids on the activity of green crab alkaline phosphatase have been studied. The results show that these derivatives of amino acids can lead to reversible inactivation. The equilibrium constants for inhibitors binding with the enzyme and/or the enzyme-substrate complexes have been determined. The obtained results show that both N-thiophosphoryl-Cys and N-thiophosphoryl-Glu were non-competitive inhibitors, while other five N-thiophosphoryl amino acids were un-competitive inhibitors. For the un-competitive inhibitors, the inhibition strength follows the order N-thiophosphoryl-Ile > -Val > -Lys > -Ala > -Tyr. Compared with respective free amino acids, it can be seen that N-thiophosphorylation of the amino acids inc-eased their inhibition strength except the N-thiophosphoryl-Cys.zh_CN
dc.language.isoen_USzh_CN
dc.subjectPHOSPHORYL GROUP PARTICIPATIONzh_CN
dc.subjectINHIBITIONzh_CN
dc.subjectKINETICSzh_CN
dc.titleThe effects of N-thiophosphoryl amino acids on the activity of green crab (Scylla Serrata) alkaline phosphatasezh_CN
dc.typeArticlezh_CN


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