| Author | Search for: Brisson, J.; Search for: Carey, P.; Search for: Storer, A. |
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| Format | Text, Article |
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| Subject | 13C; 13C-NMR; Acetonitriles; ACTIVE-SITE; Binding Sites; chemistry; Cysteine; ENZYME; Form; FORMS; Imidoesters; INTERMEDIATE; Magnetic Resonance Spectroscopy; metabolism; MODEL; Nitrogen; NMR; NMR spectroscopy; NMR-spectroscopy; Papain; SITE; SPECTROSCOPY; STATE; structure; Sulfhydryl Compounds; TRANSITION |
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| Abstract | 13C NMR spectroscopy has been used to demonstrate that 13CN-labeled benzoylamidoacetonitrile forms a covalent adduct with the thiol group of cysteine 25 in the active site of papain. Spectral comparison with model compounds indicates that the adduct is a thioimidate. On the basis of a proposed mechanism for the formation of the thioimidate, it is concluded that the -CH2C(= NH)S--imino nitrogen does not sit in the active site in the same manner as the thiol ester carbonyl oxygen of the thiol acyl enzyme (or the oxyanion of the tetrahedral intermediate). Thus, in this sense the stabilization of the thioimidate does not reflect a similarity in structure between the bound thioimidate and the transition state |
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| Publication date | 1986-07-15 |
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| In | |
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| Language | English |
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| NRC number | BRISSON1986B |
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| NPARC number | 9382890 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 3c5f2bba-6b71-41ae-8050-0113804106fb |
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| Record created | 2009-07-10 |
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| Record modified | 2020-03-17 |
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