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Essential tyrosyl residues in Lactobacillus casei thymidylate synthetase |
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| Authors: | D Rosson H B Otwell R B Dunlap |
| Institution: | Department of Chemistry University of South Carolina Columbia, South Carolina 29208 USA |
| Abstract: | Sulfhydryl-blocked thymidylate synthetase (EC 2.1.1.4.5) is rapidly inactivated by low concentrations of tetranitromethane. This reagent first nitrates two non-essential tyrosines per dimeric enzyme molecule followeed by two essential tyrosines with no oxidation of sulfhydryl groups. dUMP affords significant protection against inactivation. These results suggest that essential tyrosyl residues are present in the active sites of the enzyme. |
| Keywords: | ± 5 10-methylenetetrahydrofolate FdUMP 5-fluoro-2′-deoxyuridylate DTNB 5 5′-dithiobis(2-nitrobenzoic acid) MMTS methyl methanethiolsulfonate DTE dithioerythreitol pHMB SDS sodium dodecyl sulfate |
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