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Literature summary extracted from

  • Hans, M.; Buckel, W.; Bill, E.
    The iron-sulfur clusters in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Biochemical and spectroscopic investigations (2000), Eur. J. Biochem., 267, 7082-7093.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.167 Acidaminococcus fermentans P11569 and P11570 and P11568 P11569 i.e. subunit alpha, P11570 i.e. subunit beta, P11568 i.e. activator protein
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4.2.1.167 Acidaminococcus fermentans DSM 20731 P11569 and P11570 and P11568 P11569 i.e. subunit alpha, P11570 i.e. subunit beta, P11568 i.e. activator protein
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Storage Stability

EC Number Storage Stability Organism
4.2.1.167 homodimeric activator, in the presence of 5 mM MgCl2 and 1 mM ADP or ATP, can be stabilized and stored for 4 days at 4°C without loss of activity Acidaminococcus fermentans

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.167 riboflavin presence of trace amounts Acidaminococcus fermentans
4.2.1.167 riboflavin 5'-phosphate 1 mol per mol of heterodimeric dehydratase Acidaminococcus fermentans
4.2.1.167 [4Fe-4S]-center each active component contains an oxygen sensitive diamagnetic [4Fe-4S]2+ cluster. Reduction of the [4Fe-4S]2+ cluster of the activator protein with dithionite yields a paramagnetic [4Fe-4S]1+ cluster with the unusual electron spin ground state S=3/2. Under air the activator protein looses its activity within seconds due to irreversible degradation of its [4Fe-4S]2+ cluster to a [2Fe-2S]2+ cluster. The [4Fe-4S]2+ cluster of the heterodimeric dehydratase cannot be reduced to a [4Fe-4S]1+ cluster Acidaminococcus fermentans