A novel reaction of S-adenosyl-L-methionine correlated with the activation of pyruvate formate-lyase |
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Authors: | Joachim Knappe Thomas Schmitt |
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Institution: | Institut für Biologische Chemie der Universität Heidelberg D-69 Heidelberg, Federal Republic of Germany |
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Abstract: | Conversion of the inactive form of pyruvate formate-lyase to the catalytically active enzyme is accomplished by the Fe-dependent ‘enzyme II’; reduced flavodoxin, S-adenosyl-L-methionine and the effector pyruvate are required. It was found that adenosylmethionine is reductively processed during activation of pyruvate formate-lyase to yield methionine, adenine and 5-deoxyribose. We suggest that transient adenosylation of enzyme II is required for its function as a converter enzyme. |
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Keywords: | active forms of pyruvate formate-lyase inactive forms of pyruvate formate-lyase Fld flavodoxin |
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