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Literature summary extracted from

  • Reyda, M.R.; Dippold, R.; Dotson, M.E.; Jarrett, J.T.
    Loss of iron-sulfur clusters from biotin synthase as a result of catalysis promotes unfolding and degradation (2008), Arch. Biochem. Biophys., 471, 32-41.
    View publication on PubMedView publication on EuropePMC

General Stability

EC Number General Stability Organism
2.8.1.6 loss of the [2Fe-2S]2+ cluster from BioB does not result in global unfolding of the polypeptide chain at 20°C and does not result in significant destabilization of the dimer interface Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.8.1.6 Iron BioB appears to be resistant to degradation and capable of multiple turnovers only under high-iron conditions that favor repair of the FeS clusters, a process most likely mediated by the Isc or Suf iron-sulfur cluster assembly systems. Escherichia coli
2.8.1.6 Iron loss of the FeS clusters results in decreased thermal stability and apparent localized unfolding of BioB, particularly in the regions around Arg168 and Arg245, but not global unfolding Escherichia coli
2.8.1.6 Iron the [2Fe-2S]2+ cluster is both the sulfur-donating substrate and the sulfur-oxidizing cofactor Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.1.6 dethiobiotin + sulfur Escherichia coli biotin synthase is active for only one turnover, during which the [2Fe-2S]2+ cluster is destroyed, one sulfide from the cluster is incorporated as the biotin thiophane sulfur, while Fe2+ ions and the remaining S2- ion are released from the protein biotin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.6 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.1.6
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.6 dethiobiotin + sulfur biotin synthase is active for only one turnover, during which the [2Fe-2S]2+ cluster is destroyed, one sulfide from the cluster is incorporated as the biotin thiophane sulfur, while Fe2+ ions and the remaining S2- ion are released from the protein Escherichia coli biotin
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.1.6 dimer 2Fe-BioB, 92800, 86% dimer, equilibrium analytical ultracentrifugation Escherichia coli
2.8.1.6 More 2Fe-BioB, 188200, 14% tetramer, equilibrium analytical ultracentrifugation, tetrameric BioB is less active than dimeric enzyme, and it is assumed that the more abundant and active dimer reflects the native quaternary structure Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.8.1.6 BioB
-
 Escherichia coli
2.8.1.6 biotin synthase
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.8.1.6 additional information
-
 The loss of each FeS cluster results in a corresponding moderate decrease in the thermal stability, loss of the [4Fe-4S]2+ cluster and the bound substrates results in a 7°C decrease in stability Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.8.1.6 additional information
-
 additional information BioB is active for only one turnover, during which the [2Fe-2S]2+ cluster is destroyed, one sulfide from the cluster is incorporated as the biotin thiophane sulfur, while Fe2+ ions and the remaining S2- ion are released from the protein Escherichia coli