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Literature summary for 2.8.1.6 extracted from

  • Abdel-Hamid, A.M.; Cronan, J.E.
    In vivo resolution of conflicting in vitro results: Synthesis of biotin from dethiobiotin does not require pyridoxal phosphate (2007), Chem. Biol., 14, 1215-1220.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
The delta pdxH::CAT allele of strain TX2767 is transduced into strain ER47 with phage P1vir to give strain AH14 into which plasmids pER30 and pER35 are introduced Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dethiobiotin + sulfur + 2 S-adenosyl-L-methionine Escherichia coli The biotin synthase (BioB) reaction does not require pyridoxal phosphate in vivo. Therefore, the biotin sulfur atom cannot be derived via an intrinsic pyridoxal phosphate-dependent BioB cysteine desulfurase activity biotin + 2 L-methionine + 2 5'-deoxyadenosine
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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host strain is blocked in the synthesis of pyridoxal (due to a null deletion/insertion mutation of pdxH which encodes pyridoxine 5’-phosphate oxidase)
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dethiobiotin + sulfur + 2 S-adenosyl-L-methionine The biotin synthase (BioB) reaction does not require pyridoxal phosphate in vivo. Therefore, the biotin sulfur atom cannot be derived via an intrinsic pyridoxal phosphate-dependent BioB cysteine desulfurase activity Escherichia coli biotin + 2 L-methionine + 2 5'-deoxyadenosine
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Synonyms

Synonyms Comment Organism
BioB
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Escherichia coli
biotin synthase
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Escherichia coli