Pimeloyl-[acyl-carrier protein] methyl ester esterase
Details
- Name
- Pimeloyl-[acyl-carrier protein] methyl ester esterase
- Synonyms
- 3.1.1.85
- bioB
- Biotin synthesis protein BioH
- Carboxylesterase BioH
- Gene Name
- bioH
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011159|Pimeloyl-[acyl-carrier protein] methyl ester esterase MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALS LADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGI KPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLALPMPEVDVLNGGL EILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS HPAEFCHLLVALKQRV
- Number of residues
- 256
- Molecular Weight
- 28504.785
- Theoretical pI
- 7.02
- GO Classification
- Functionscarboxylic ester hydrolase activity / pimelyl-[acyl-carrier protein] methyl ester esterase activityProcessesbiotin biosynthetic processComponentscytoplasm
- General Function
- Pimelyl-[acyl-carrier protein] methyl ester esterase activity
- Specific Function
- 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.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.
- Pfam Domain Function
- Abhydrolase_1 (PF00561)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011160|Pimeloyl-[acyl-carrier protein] methyl ester esterase (bioH) ATGAATAACATCTGGTGGCAGACCAAAGGTCAGGGGAATGTTCATCTTGTGCTGCTGCAC GGATGGGGACTGAATGCCGAAGTGTGGCGTTGCATTGACGAGGAACTTAGCTCGCATTTT ACGCTGCACCTTGTTGACCTGCCCGGCTTCGGGCGTAGCCGGGGATTTGGTGCGCTGTCA CTTGCTGATATGGCCGAAGCCGTGCTGCAACAGGCACCTGATAAAGCCATTTGGTTAGGC TGGAGTCTGGGCGGGCTGGTGGCAAGCCAGATTGCGTTAACCCATCCCGAGCGTGTTCAG GCGCTGGTCACCGTGGCGTCGTCACCTTGTTTTAGTGCTCGTGACGAGTGGCCGGGGATA AAACCGGACGTGCTGGCGGGATTTCAGCAGCAACTCAGTGATGATTTTCAGCGTACAGTG GAGCGGTTCCTGGCGTTACAAACCATGGGGACTGAAACGGCGCGCCAGGATGCGCGGGCG TTGAAGAAAACCGTTCTGGCGTTACCGATGCCGGAGGTTGACGTGCTTAATGGCGGGCTG GAAATCCTGAAAACGGTCGATCTCCGTCAGCCGCTGCAAAACGTGTCCATGCCGTTTTTG CGATTGTATGGCTATCTCGACGGTCTGGTGCCGCGCAAAGTGGTGCCGATGCTGGATAAA CTTTGGCCTCACAGCGAATCATATATCTTCGCCAAAGCGGCCCATGCGCCATTTATTTCG CATCCGGCCGAGTTTTGTCACCTGCTGGTGGCGTTGAAGCAGAGGGTGTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P13001 UniProtKB Entry Name BIOH_ECOLI GenBank Protein ID 41068 GenBank Gene ID X15587 - General References
- O'Regan M, Gloeckler R, Bernard S, Ledoux C, Ohsawa I, Lemoine Y: Nucleotide sequence of the bioH gene of Escherichia coli. Nucleic Acids Res. 1989 Oct 11;17(19):8004. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- 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. [Article]
- 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. [Article]
- Kwon MA, Kim HS, Oh JY, Song BK, Song JK: Gene cloning, expression, and characterization of a new carboxylesterase from Serratia sp. SES-01: comparison with Escherichia coli BioHe enzyme. J Microbiol Biotechnol. 2009 Feb;19(2):147-54. [Article]
- 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. [Article]
- 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. [Article]