The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and a putative dethiobiotinyl carbon radical.,
In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis.,
Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-(S) hydrogen atom from 9-mercaptodethiobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring.,
The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster.,
The sulfur donor (S) is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover.
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| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
Biotin synthase
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| uniprot:activity |
Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine.
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| uniprot:cofactor |
Iron-sulfur
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