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Mutagenesis of the proposed iron‐sulfur cluster binding ligands in Escherichia coli biotin synthase
[摘要]

Biotin synthase (BioB) is a member of a family of enzymes that includes anaerobic ribonucleotide reductase and pyruvate formate lyase activating enzyme. These enzymes all use S-adenosylmethionine during turnover and contain three highly conserved cysteine residues that may act as ligands to an iron-sulfur cluster required for activity. Three mutant enzymes of BioB have been made, each with one cysteine residue (C53, 57, 60) mutated to alanine. All three mutant enzymes were inactive, but they still exhibited the characteristic UV-visible spectrum of a [2Fe-2S]2+ cluster similar to that of the wild-type enzyme.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] Biotin synthase;Iron-sulfur cluster;Mutagenesis of iron-sulfur cluster ligand;SAM;S-adenosylmethionine;Fe-S;iron-sulfur cluster;DTT;dithiothreitol;SDS–PAGE;sodium dodecyl sulfate–polyacrylamide gel electrophoresis;pfl AE;pyruvate formate lyase activating enzyme;aRR AE;anaerobic ribonucleotide reductase activating enzyme [时效性] 
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