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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.8.1.6 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
2.8.1.6 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
2.8.1.6 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
2.8.1.6 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
2.8.1.6 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
2.8.1.6 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
2.8.1.6 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
2.8.1.6 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)

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

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.1.6 37
-
 activity assay Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.1.6 8
-
 activity assay Escherichia coli

Cofactor

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

General Information

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