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
Functions
carboxylic ester hydrolase activity / pimelyl-[acyl-carrier protein] methyl ester esterase activity
Processes
biotin biosynthetic process
Components
cytoplasm
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
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
ResourceLink
UniProtKB IDP13001
UniProtKB Entry NameBIOH_ECOLI
GenBank Protein ID41068
GenBank Gene IDX15587
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03688Hydracrylic acidexperimentalunknownDetails