| Structural highlights
Function
BIOH_ECOLI The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain p-nitrophenyl esters. Also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis.[1] [2] [3] [4] Catalyzes the hydrolysis of the methyl ester bond of dimethylbutyryl-S-methyl mercaptopropionate (DMB-S-MMP) to yield dimethylbutyryl mercaptopropionic acid (DMBS-MPA) during the biocatalytic conversion of simvastin acid from monacolin J acid. Can also use acyl carriers such as dimethylbutyryl-S-ethyl mercaptopropionate (DMB-S-EMP) and dimethylbutyryl-S-methyl thioglycolate (DMB-S-MTG) as the thioester substrates.[5] [6] [7] [8]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Tomczyk NH, Nettleship JE, Baxter RL, Crichton HJ, Webster SP, Campopiano DJ. Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway. FEBS Lett. 2002 Feb 27;513(2-3):299-304. PMID:11904168
- ↑ Xie X, Wong WW, Tang Y. Improving simvastatin bioconversion in Escherichia coli by deletion of bioH. Metab Eng. 2007 Jul;9(4):379-86. Epub 2007 Jun 5. PMID:17625941 doi:http://dx.doi.org/10.1016/j.ymben.2007.05.006
- ↑ Lin S, Hanson RE, Cronan JE. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat Chem Biol. 2010 Sep;6(9):682-8. doi: 10.1038/nchembio.420. Epub 2010 Aug 8. PMID:20693992 doi:http://dx.doi.org/10.1038/nchembio.420
- ↑ Sanishvili R, Yakunin AF, Laskowski RA, Skarina T, Evdokimova E, Doherty-Kirby A, Lajoie GA, Thornton JM, Arrowsmith CH, Savchenko A, Joachimiak A, Edwards AM. Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli. J Biol Chem. 2003 Jul 11;278(28):26039-45. Epub 2003 May 5. PMID:12732651 doi:10.1074/jbc.M303867200
- ↑ Tomczyk NH, Nettleship JE, Baxter RL, Crichton HJ, Webster SP, Campopiano DJ. Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway. FEBS Lett. 2002 Feb 27;513(2-3):299-304. PMID:11904168
- ↑ Xie X, Wong WW, Tang Y. Improving simvastatin bioconversion in Escherichia coli by deletion of bioH. Metab Eng. 2007 Jul;9(4):379-86. Epub 2007 Jun 5. PMID:17625941 doi:http://dx.doi.org/10.1016/j.ymben.2007.05.006
- ↑ Lin S, Hanson RE, Cronan JE. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat Chem Biol. 2010 Sep;6(9):682-8. doi: 10.1038/nchembio.420. Epub 2010 Aug 8. PMID:20693992 doi:http://dx.doi.org/10.1038/nchembio.420
- ↑ Sanishvili R, Yakunin AF, Laskowski RA, Skarina T, Evdokimova E, Doherty-Kirby A, Lajoie GA, Thornton JM, Arrowsmith CH, Savchenko A, Joachimiak A, Edwards AM. Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli. J Biol Chem. 2003 Jul 11;278(28):26039-45. Epub 2003 May 5. PMID:12732651 doi:10.1074/jbc.M303867200
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