Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.1 Carboxylic-ester hydrolases
ID:3.1.1.85
Description:Pimeloyl-[acyl-carrier protein] methyl ester esterase.
Cath: 3.40.50.1820;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.1.85
BRENDA Enzyme Link: BRENDA 3.1.1.85
KEGG Enzyme Link: KEGG3.1.1.85
BioCyc Enzyme Link: BioCyc 3.1.1.85
ExPASy Enzyme Link: ExPASy3.1.1.85
EC2PDB Enzyme Link: EC2PDB 3.1.1.85
ExplorEnz Enzyme Link: ExplorEnz 3.1.1.85
PRIAM enzyme-specific profiles Link: PRIAM 3.1.1.85
IntEnz Enzyme Link: IntEnz 3.1.1.85
MEDLINE Enzyme Link: MEDLINE 3.1.1.85
MSA:

3.1.1.85;

Phylogenetic Tree:

3.1.1.85;

Uniprot:
M-CSA:
RHEA:42700 H2O + pimeloyl-[ACP] methyl ester = H(+) + methanol + pimeloyl-[ACP]
RULE(radius=1) [*:1]-[O;H0;+0:2]-[CH3;+0:3].[OH2;+0:4]>>[*:1]-[OH;+0:2].[CH3;+0:3]-[OH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Biotin synthesis begins by hijacking the fatty acid synthetic pathway.Lin S, Hanson RE, Cronan JE2010 Sep20693992
Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli.Sanishvili R, Yakunin AF, Laskowski RA, Skarina T, Evdokimova E, Doherty-Kirby A, Lajoie GA, Thornton JM, Arrowsmith CH, Savchenko A, Joachimiak A, Edwards AM2003 Jul 1112732651
Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway.Tomczyk NH, Nettleship JE, Baxter RL, Crichton HJ, Webster SP, Campopiano DJ2002 Feb 2711904168