Abstract:
:The forms of Se in the Se-dependent enzyme formate dehydrogenase is known to be selenocysteine, but the way this amino acid enters the polypeptide chain has not been established. Through the use of a cysteine-requiring mutant ofEscherichia coli K-12 that could also grow in the presence of glutathione, we were able to study the effect of selenite, selenide, andL-selenocysteine, each at a concentration of 0.1 μM, on the synthesis of formate dehydrogenase. The three forms of Se served equally well for inducing formate dehydrogenase activity, measured by dichlorophenol-indophenol reduction mediated by phenazine methosulfate. It is known that selenite can be reduced to selenide by the action of glutathione reductase, present inE. coli, and that selenocysteine is converted to elemental Se by the action of selenocysteine lyase, also present in the mutant. Elemental Se is then reduced nonenzymatically to hydrogen selenide. The conversion of both selenite and selenocysteine to selenide and the ability of each form of Se to induce the synthesis of equal levels of formate dehydrogenase suggest that the incorporation of Se into formate dehydrogenase is accomplished by a posttranslational mechanism.
journal_name
Biol Trace Elem Resjournal_title
Biological trace element researchauthors
Karle JA,Shrift Adoi
10.1007/BF02795520subject
Has Abstractpub_date
1986-12-01 00:00:00pages
27-35issue
1eissn
0163-4984issn
1559-0720journal_volume
11pub_type
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pub_type: 杂志文章,评审
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pub_type: 杂志文章,meta分析
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pub_type: 杂志文章,评审
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