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Information on EC 3.1.1.85 - pimelyl-[acyl-carrier protein] methyl ester esterase and Organism(s) Escherichia coli and UniProt Accession P13001

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IUBMB Comments
Involved in biotin biosynthesis in Gram-negative bacteria. The enzyme exhibits carboxylesterase activity, particularly toward substrates with short acyl chains [1,2]. Even though the enzyme can interact with coenzyme A thioesters , the in vivo role of the enzyme is to hydrolyse the methyl ester of pimeloyl-[acyl carrier protein], terminating the part of the biotin biosynthesis pathway that is catalysed by the fatty acid elongation enzymes .
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This record set is specific for:
Escherichia coli
UNIPROT: P13001
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
bioh protein, pimeloyl-acp methyl esterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
pimelyl-[acyl-carrier protein] methyl ester hydrolase
Involved in biotin biosynthesis in Gram-negative bacteria. The enzyme exhibits carboxylesterase activity, particularly toward substrates with short acyl chains [1,2]. Even though the enzyme can interact with coenzyme A thioesters [3], the in vivo role of the enzyme is to hydrolyse the methyl ester of pimeloyl-[acyl carrier protein], terminating the part of the biotin biosynthesis pathway that is catalysed by the fatty acid elongation enzymes [4].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
?
show the reaction diagram
highest carboxylesterase activity
-
-
?
4-nitrophenyl butyrate + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl caprate + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl caproate + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl laurate + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl palmitate + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl propionate + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl stearate + H2O
?
show the reaction diagram
very low carboxylesterase activity
-
-
?
pimelyl-[acyl-carrier protein] methyl ester + H2O
pimelyl-[acyl-carrier protein] + methanol
show the reaction diagram
-
-
-
?
adipyl-[acyl-carrier protein] methyl ester + H2O
adipyl-[acyl-carrier nprotein] + methanol
show the reaction diagram
-
-
-
-
?
azelayl-[acyl-carrier protein] methyl ester + H2O
azelayl-[acyl-carrier protein] + methanol
show the reaction diagram
-
-
-
-
?
pimeloyl-[acyl-carrier protein] butyl ester + H2O
pimeloyl-[acyl-carrier protein] + butanol
show the reaction diagram
-
-
-
-
?
pimeloyl-[acyl-carrier protein] ethyl ester + H2O
pimeloyl-[acyl-carrier protein] + ethanol
show the reaction diagram
-
-
-
-
?
pimeloyl-[acyl-carrier protein] methyl ester + H2O
pimeloyl-[acyl-carrier protein] + methanol
show the reaction diagram
-
-
-
-
?
pimeloyl-[acyl-carrier protein] propyl ester + H2O
pimeloyl-[acyl-carrier protein] + propanol
show the reaction diagram
-
-
-
-
?
suberyl-[acyl-carrier protein] methyl ester + H2O
suberyl-[acyl-carrier protein] + methanol
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phenylmethylsulfonyl fluoride
10.5% residual activity after 10 min of incubation with 2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
4-nitrophenyl acetate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
0.33
4-nitrophenyl butyrate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
0.25
4-nitrophenyl caproate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
0.6
4-nitrophenyl laurate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
0.35
4-nitrophenyl propionate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.5
4-nitrophenyl acetate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
6.1
4-nitrophenyl butyrate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
4
4-nitrophenyl caproate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
1.5
4-nitrophenyl laurate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
13.1
4-nitrophenyl propionate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
63.8
4-nitrophenyl acetate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
18.5
4-nitrophenyl butyrate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
16
4-nitrophenyl caproate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
2.5
4-nitrophenyl laurate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
37.4
4-nitrophenyl propionate
in 50 mM HEPES-K (pH 7.5) buffer, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
BioH is involved in biotin biosynthesis
metabolism
-
the bioH gene product is required for the synthesis of pimeloyl-CoA
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
SDS-PAGE
28510
-
calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.2 M sodium citrate trihydrate and 0.1 M Tris-HCl (pH 8.0), at 21°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S53A
-
the mutant is insoluble
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
Q-Sepharose column chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in the Escherichia coli auxotroph strain B834 (DE3)
expressed in Escherichia coli Hms174(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sanishvili, R.; Yakunin, A.F.; Laskowski, R.A.; Skarina, T.; Evdokimova, E.; Doherty-Kirby, A.; Lajoie, G.A.; Thornton, J.M.; Arrowsmith, C.H.; Savchenko, A.; Joachimiak, A.; Edwards, A.M.
Integrating structure, bioinformatics, and enzymology to discover function. BioH, a new carboxylesterase from Escherichia coli
J. Biol. Chem.
278
26039-26045
2003
Escherichia coli (P13001), Escherichia coli DH5-alpha (P13001)
Manually annotated by BRENDA team
Lin, S.; Hanson, R.E.; Cronan, J.E.
Biotin synthesis begins by hijacking the fatty acid synthetic pathway
Nat. Chem. Biol.
6
682-688
2010
Escherichia coli
Manually annotated by BRENDA team
Tomczyk, N.H.; Nettleship, J.E.; Baxter, R.L.; Crichton, H.J.; Webster, S.P.; Campopiano, D.J.
Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway
FEBS Lett.
513
299-304
2002
Escherichia coli, Escherichia coli JM101, Neisseria meningitidis, Neisseria meningitidis H44/76
Manually annotated by BRENDA team