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Literature summary for 2.8.1.6 extracted from

  • Farrar, C.; Jarrett, J.
    Protein residues that control the reaction trajectory in S-adenosylmethionine radical enzymes: Mutagenesis of asparagine 153 and aspartate 155 in Escherichia coli biotin synthase (2009), Biochemistry, 48, 2448-2458.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
hexahistidine tagged proteins are expressed in Escherichia coli BL21DE3 pLysS cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
D155A mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet Escherichia coli
D155E mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet Escherichia coli
D155N mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet Escherichia coli
D155S mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet Escherichia coli
N153A mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet Escherichia coli
N153D mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet Escherichia coli
N153Q mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet Escherichia coli
N153S mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dethiobiotin + sulfur + S-adenosyl-L-methionine Escherichia coli
-
biotin + L-methionine + 5'-deoxyadenosine
-
?

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 + S-adenosyl-L-methionine
-
Escherichia coli biotin + L-methionine + 5'-deoxyadenosine
-
?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
activity assay Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
activity assay Escherichia coli

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre
-
Escherichia coli
S-adenosyl-L-methionine
-
Escherichia coli

General Information

General Information Comment Organism
physiological function biotin synthase is an AdoMet radical enzyme that catalyses the final step in the biosynthesis of biotin Escherichia coli