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Literature summary extracted from

  • Lin, S.; Hanson, R.E.; Cronan, J.E.
    Biotin synthesis begins by hijacking the fatty acid synthetic pathway (2010), Nat. Chem. Biol., 6, 682-688.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.197 additional information construction of the DELTAbioC deletion mutant, that is only able to grow in biotin and derivative supplemented medium. Escherichia coli strain ER90 DELTAbioF bioC bioD carries an insertion-deletion mutation within bioF that also inactivates the downstream genes, bioC and bioD, by transcriptional polarity Escherichia coli
3.1.1.85 S82A inactive Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.197 S-adenosyl-L-methionine + malonyl-CoA Escherichia coli
-
 S-adenosyl-L-homocysteine + malonyl-CoA methyl ester the methyl ester moiety is essential for chain elongation ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.197 Escherichia coli
-
-
-
2.1.1.197 Escherichia coli
-
 gene bioC
-
3.1.1.85 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.197 S-adenosyl-L-methionine + malonyl-CoA
-
 Escherichia coli S-adenosyl-L-homocysteine + malonyl-CoA methyl ester
-
 ?
2.1.1.197 S-adenosyl-L-methionine + malonyl-CoA
-
 Escherichia coli S-adenosyl-L-homocysteine + malonyl-CoA methyl ester the methyl ester moiety is essential for chain elongation ?
3.1.1.85 adipyl-[acyl-carrier protein] methyl ester + H2O
-
 Escherichia coli adipyl-[acyl-carrier nprotein] + methanol
-
 ?
3.1.1.85 azelayl-[acyl-carrier protein] methyl ester + H2O
-
 Escherichia coli azelayl-[acyl-carrier protein] + methanol
-
 ?
3.1.1.85 additional information BioH fails to cleave malonyl-[acyl-carrier protein] methyl ester and succinyl-[acyl-carrier protein] methyl ester Escherichia coli ?
-
 ?
3.1.1.85 pimeloyl-[acyl-carrier protein] butyl ester + H2O
-
 Escherichia coli pimeloyl-[acyl-carrier protein] + butanol
-
 ?
3.1.1.85 pimeloyl-[acyl-carrier protein] ethyl ester + H2O
-
 Escherichia coli pimeloyl-[acyl-carrier protein] + ethanol
-
 ?
3.1.1.85 pimeloyl-[acyl-carrier protein] methyl ester + H2O
-
 Escherichia coli pimeloyl-[acyl-carrier protein] + methanol
-
 ?
3.1.1.85 pimeloyl-[acyl-carrier protein] propyl ester + H2O
-
 Escherichia coli pimeloyl-[acyl-carrier protein] + propanol
-
 ?
3.1.1.85 suberyl-[acyl-carrier protein] methyl ester + H2O
-
 Escherichia coli suberyl-[acyl-carrier protein] + methanol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.197 BioC
-
 Escherichia coli
2.1.1.197 S-adenosyl-L-methionine-dependent methyltransferase
-
 Escherichia coli
2.1.1.197 SAM-dependent methyltransferase
-
 Escherichia coli
3.1.1.85 BioH
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.197 S-adenosyl-L-methionine
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.1.1.197 malfunction the DELTAbioC deletion mutant is only able to grow in biotin supplemented medium. Also supplementation with pimelic acid, and putative intermediates in the pathway, the enoyl, 3-keto and 3-hydroxy derivatives of the monomethyl ester of glutarate and the 3-keto and 3-hydroxy derivatives of the monomethyl ester of pimelate, allow growth of the mutant strain in the absence of biotin, but the 2-keto, 2-hydroxy and 4-keto derivatives, as well as monomethyl esters of C4, C6, C8, C9 and C11 dicarboxylates, do not, overview Escherichia coli
2.1.1.197 metabolism the pimeloyl moiety of biotin is synthesized by a modified fatty acid synthetic pathway in which the omega-carboxyl group of a malonyl-thioester is methylated by BioC which allows recognition of this atypical substrate by the fatty acid synthetic enzymes. The malonyl-thioester methyl ester enters fatty acid synthesis as the primer and undergoes two reiterations of the fatty acid elongation cycle to give pimeloyl-acyl carrier protein methyl ester which is hydrolyzed to pimeloyl-ACP and methanol by BioH Escherichia coli
2.1.1.197 physiological function in biotin synthesis, the pimeloyl moiety is synthesized by a modified fatty acid synthetic pathway in which the omega-carboxyl group of a malonyl-thioester is methylated by BioC, which allows recognition of this atypical substrate by the fatty acid synthetic enzymes. The malonyl-thioester methyl ester enters fatty acid synthesis as the primer and undergoes two reiterations of the fatty acid elongation cycle to give pimeloyl-acyl carrier protein methyl ester. Supplementation of biotin-free medium with any of malonic, glutaric and pimelic acid monomethyl ester allows for acyl-ACP-synthetase-dependent growth of the bioC deletion strain Escherichia coli
2.1.1.197 physiological function the role of BioC is to convert the free carboxyl group of a malonylthioester to its methyl ester by transfer of a methyl group from SAM. Methylation both cancels the charge of the carboxyl group and provides a methyl carbon to mimic the methyl ends of normal fatty acyl chains Escherichia coli