Stereospecificity of hydrolytic enzymes in their reaction with optically active organophosphorus compounds - II : The inhibition of aliesterase, acetylesterase, chymotrypsin and trypsin by S-alkyl p-nitrophenyl methylphosphonothiolates

article

Boter, H.L.

Ooms, A.J.J.
Rate constants of the irreversible inhibition of aliesterase, acetylesterase, chymotrypsin and trypsin by racemic and enantiomeric forms of some S-alkyi p-nitrophenyl methylphosphonothiolates were measured. Of the esterases investigated acetylesterase showed the most pronounced stereospecificity. The stereospecificity pattern corresponded with that reported previously for acetylcholinesterase. In the case of chymotrypsin an inversion of the stereospecificity throughout the enantiomeric series of inhibitors was observed. © 1967.
Chemicals/CAS: acetylesterase, 9000-82-2; chymotrypsin, 9004-07-3, 9014-64-6; esterase, 9013-79-0; trypsin inhibitor, 9035-81-8; Acetylesterase, EC 3.1.1.6; Chymotrypsin, EC 3.4.21.1; Esterases, EC 3.1.; Phosphonic Acids; Trypsin Inhibitors
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phosphonic acid derivativebinding siteBinding SitesChymotrypsinEsterasesPhosphonic AcidsTrypsin InhibitorsStereochemistryOptical activityPhosphorus organic compoundsNitro compoundsSulfur organic compoundsCholinesterase inhibitorsEnzymesEsterasesAcetylesteraseChymotrypsinTrypsinReaction kinetics
TNO Identifier
226984
Repository link
https://resolver.tno.nl/uuid:0b0ad71f-52c3-45f0-9916-5cb13dce30d8
ISSN
00062952
Source
Biochemical Pharmacology, 16(8), pp. 1563-1569.
Pages
1563-1569
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