4.2.1.167: (R)-2-hydroxyglutaryl-CoA dehydratase
This is an abbreviated version!
For detailed information about (R)-2-hydroxyglutaryl-CoA dehydratase, go to the full flat file.
Reaction
Synonyms
hgdAB, HgdC
ECTree
4.2.1.167 (R)-2-hydroxyglutaryl-CoA dehydrataseAdvanced search results
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results (Cofactor
Cofactor on EC 4.2.1.167 - (R)-2-hydroxyglutaryl-CoA dehydratase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Ferredoxin
alternative electron donor besides flavodoxin is a two [4Fe-4S]1+/2+-cluster-containing ferredoxin, with redox potentials of 405 mV and 340mV. The flavodoxin is the dominant electron donor protein under iron-limiting conditions. The concentration of ferredoxin increases stepwise from about 0.2 micromol/g at 713 microM Fe to 1.1 micromol/g at 1745 microM Fe
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flavodoxin
dominant electron donor protein under iron-limiting conditions
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riboflavin 5'-phosphate
1 mol per mol of heterodimeric dehydratase
riboflavin 5'-phosphate
the actual dehydration is mediated by component D, which contains 1.0 [4Fe-4S]2+ cluster, 1.0 reduced riboflavin-5'-phosphate and about 0.1 molybdenum (VI) per heterodimer
riboflavin 5'-phosphate
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
the enzyme contains 1.0 mol of riboflavin 5'-phosphate per mol of heterodimeric enzyme
[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
[4Fe-4S]-center
the actual dehydration is mediated by component D, which contains 1.0 [4Fe-4S]2+ cluster, 1.0 reduced riboflavin-5'-phosphate and about 0.1 molybdenum (VI) per heterodimer
[4Fe-4S]-center
the reduced [4Fe-4S]+ cluster containing activator protein transfers one electron to the dehydratase driven by ATP hydrolysis, which activates the enzyme. With a tenfold excess of titanium(III) citrate at pH 8.0 the activator can be further reduced, yielding about 50% of a superreduced [4Fe-4S]0 cluster in the all-ferrous state. The superreduced cluster has apparent spectroscopic similarities with the corresponding [4Fe-4S]0 cluster described for the nitrogenase Fe-protein. Only one-electron transfer steps are involved in dehydratase catalysis
[4Fe-4S]-center
the [4Fe-4S](1+/2+) cluster of the activator protein is exposed to the solvent. Upon exchange of the bound ADP by ATP, the chelation rate by iron chelators is 8fold enhanced, indicating a large conformational change. Oxidized activator exhibits ATPase activity of 6 s(-1), which is completely abolished upon reduction by one electron
