| IED ID | IndEnz0010000224 |
| Enzyme Type ID | esterase000224 |
| Protein Name |
Pimeloyl- acyl-carrier protein methyl ester esterase EC 3.1.1.85 Biotin synthesis protein BioH Carboxylesterase BioH |
| Gene Name | bioH bioB b3412 JW3375 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPAEFCHLLVALKQRV |
| Enzyme Length | 256 |
| Uniprot Accession Number | P13001 |
| Absorption | |
| Active Site | ACT_SITE 82; /note=Nucleophile; ACT_SITE 207; /evidence=ECO:0000250; ACT_SITE 235 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by phenylmethylsulfonyl fluoride (PMSF). |
| Binding Site | BINDING 22; /note=Substrate; via amide nitrogen and carbonyl oxygen; BINDING 235; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol; Xref=Rhea:RHEA:42700, Rhea:RHEA-COMP:9955, Rhea:RHEA-COMP:10186, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:78846, ChEBI:CHEBI:82735; EC=3.1.1.85; Evidence={ECO:0000269|PubMed:11904168}; |
| DNA Binding | |
| EC Number | 3.1.1.85 |
| Enzyme Function | 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.; FUNCTION: 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. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 20 and 30 degrees Celsius. {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. The activity is more than 90% in the pH range from 7 to 9. {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; |
| Pathway | PATHWAY: Cofactor biosynthesis; biotin biosynthesis. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (8); Binding site (2); Chain (1); Domain (1); Helix (12); Mutagenesis (1); Region (2) |
| Keywords | 3D-structure;Biotin biosynthesis;Cytoplasm;Hydrolase;Reference proteome;Serine esterase |
| Interact With | P0A6A8 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1M33; |
| Mapped Pubmed ID | 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,505 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=229 uM for DMB-S-MMP (at Ph 7.9 and at room temperature) {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; KM=0.29 mM for pNP-acetate {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; KM=0.35 mM for pNP-propionate {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; KM=0.33 mM for pNP-butyrate {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; KM=0.25 mM for pNP-caproate {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; KM=0.60 mM for pNP-laurate {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; Note=The highest catalytic efficiency was observed with pNP-acetate, then with pNP-propionate, pNP-butyrate and pNP-caproate.; |
| Metal Binding | |
| Rhea ID | RHEA:42700 |
| Cross Reference Brenda | 3.1.1.1;3.1.1.85; |