Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.8.1.6 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
Search for more literature for 2.8.1.6

General Stability

General Stability Organism
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

Metals/Ions Comment Organism Structure
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
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
Iron the [2Fe-2S]2+ cluster is both the sulfur-donating substrate and the sulfur-oxidizing cofactor Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Subunits Comment Organism
dimer 2Fe-BioB, 92800, 86% dimer, equilibrium analytical ultracentrifugation Escherichia coli
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

Synonyms Comment Organism
BioB
-
 Escherichia coli
biotin synthase
-
 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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