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Literature summary extracted from

  • Delli-Bovi, T.; Spalding, M.; Prigge, S.
    Overexpression of biotin synthase and biotin ligase is required for efficient generation of sulfur-35 labeled biotin in E. coli (2010), BMC Biotechnol., 10, 73.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
6.3.4.15 synthesis production of [35S]-biotin from Na-35SO4 and desthiobiotin with a specific activity of 30.7 Ci/mmol by expression of the biotinylation domain from the Plasmodium falciparum acetyl-CoA carboxylase in Escherichia coli as a biotinylation substrate. Overexpression of the biotin synthase, BioB, and biotin ligase, BirA, increases biotinylation of the biotinylation domain 160fold over basal levels. Biotinylated biotinylation domain is purified by affinity chromatography, and free biotin is liberated using acid hydrolysis Plasmodium falciparum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.1.6 expressed in Escherichia coli B834(DE3) cells Escherichia coli
6.3.4.15
-
 Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.6 Escherichia coli
-
-
-
6.3.4.15 Plasmodium falciparum C6S3D7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.6 dethiobiotin + [S] + 2 S-adenosyl-L-methionine
-
 Escherichia coli biotin + 2 L-methionine + 2 5'-deoxyadenosine
-
 ir

Synonyms

EC Number Synonyms Comment Organism
2.8.1.6 BioB
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.8.1.6 physiological function overexpression of biotin synthase is required for efficient generation of sulfur-35 labeled biotin in Escherichia coli. Coexpression of both BioB and the biotin ligase, BirA, is required for efficient biotinylation of biotin carboxy carrier protein-79 Escherichia coli