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Literature summary for 2.8.1.6 extracted from

  • Lotierzo, M.; Raux, E.; Tse Sum Bui, B.; Goasdoue, N.; Libot, F.; Florentin, D.; Warren, M.J.; Marquet, A.
    Biotin synthase mechanism: mutagenesis of the YNHNLD conserved motif (2006), Biochemistry, 45, 12274-12281.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D155A no enzymic activity, mutant is unable to cleave S-adenosyl-l-methionine and to produce the deoxyadenosyl radical Escherichia coli
H152A about 10% of turnover rate of wild-type. Ratio of 5’-deoxyadenosine to biotin is about twice as high as in wild-type Escherichia coli
N151A no enzymic activity, mutant is unable to cleave S-adenosyl-l-methionine and to produce the deoxyadenosyl radical Escherichia coli
N153A no enzymic activity, mutant is unable to cleave S-adenosyl-l-methionine and to produce the deoxyadenosyl radical Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the as-isolated form of enzyme contains an air-stable [2Fe-2S]2+ center. Enzyme can additionally accomodate an air-sensitive [4Fe-4S]2+ center which is generated by incubation under anaerobic conditions with Fe2+ and S2-. With respect to iron cluster content and characteristics, mutants N151A, H152A, N153A, D155A are similar to wild-type Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutants N151A, H152A, N153A, D155A. Purified enzymes have a reddish brown colour Escherichia coli