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ADP + heptanedioate + CoA
AMP + phosphate + heptanedioyl-CoA
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
ATP + adipate + CoA
AMP + diphosphate + adipyl-CoA
-
-
-
?
ATP + azelate + CoA
AMP + diphosphate + azelayl-CoA
-
-
-
?
ATP + glutarate + CoA
AMP + diphosphate + glutaryl-CoA
ATP + heptanedioate + CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
ATP + hexanedioate + CoA
AMP + diphosphate + hexanedioyl-CoA
ATP + nonanedioate + CoA
AMP + diphosphate + nonanedioyl-CoA
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
ATP + suberate + CoA
AMP + diphosphate + suberyl-CoA
-
-
-
?
additional information
?
-
ADP + heptanedioate + CoA
AMP + phosphate + heptanedioyl-CoA
-
85% of the activity relative to ATP
-
-
?
ADP + heptanedioate + CoA
AMP + phosphate + heptanedioyl-CoA
-
85% of the activity relative to ATP
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
best substrate
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
-
?
ATP + glutarate + CoA
AMP + diphosphate + glutaryl-CoA
-
-
-
?
ATP + glutarate + CoA
AMP + diphosphate + glutaryl-CoA
-
-
-
?
ATP + heptanedioate + CoA
?
-
-
-
-
?
ATP + heptanedioate + CoA
?
-
first enzyme of biotin biosynthesis pathway
-
-
?
ATP + heptanedioate + CoA
?
-
-
-
-
?
ATP + heptanedioate + CoA
?
-
first enzyme of biotin biosynthesis pathway
-
-
?
ATP + heptanedioate + CoA
?
Lavandula vera
-
first enzyme of biotin biosynthesis pathway
-
-
?
ATP + heptanedioate + CoA
?
-
first enzyme of biotin biosynthesis pathway
-
-
?
ATP + heptanedioate + CoA
?
-
the heptanedioyl-CoA formed in the peroxisomes is directly degraded to acetyl-CoA and malonyl-CoA by the beta-oxidation pathway
-
-
?
ATP + heptanedioate + CoA
?
-
enzyme is responsible for the first step in biotin biosynthesis by microorganisms
-
-
?
ATP + heptanedioate + CoA
?
-
enzyme is responsible for the first step in biotin biosynthesis by microorganisms
-
-
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
Lavandula vera
-
-
-
-
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
-
-
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
-
-
heptanedioyl-CoA i.e. pimelyl-CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
no activity with ethanedioate and pentanedioate
-
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
first enzyme of biotin biosynthesis pathway
-
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
no activity with ethanedioate and pentanedioate
-
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
first enzyme of biotin biosynthesis pathway
-
?
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
-
-
-
?
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
-
-
-
?
ATP + hexanedioate + CoA
AMP + diphosphate + hexanedioyl-CoA
72% activity of that for heptanedioate
-
?
ATP + hexanedioate + CoA
AMP + diphosphate + hexanedioyl-CoA
72% activity of that for heptanedioate
-
?
ATP + nonanedioate + CoA
AMP + diphosphate + nonanedioyl-CoA
18% activity of that for heptanedioate
-
?
ATP + nonanedioate + CoA
AMP + diphosphate + nonanedioyl-CoA
18% activity of that for heptanedioate
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
-
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
-
-
-
?
additional information
?
-
using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters. Azelaic acid is a poor substrate for BioW, substrate specificity and binding structures, overview
-
-
?
additional information
?
-
-
using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters. Azelaic acid is a poor substrate for BioW, substrate specificity and binding structures, overview
-
-
?
additional information
?
-
using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters. Azelaic acid is a poor substrate for BioW, substrate specificity and binding structures, overview
-
-
?
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ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
ATP + heptanedioate + CoA
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
-
?
ATP + 6-carboxyhexanoate + CoA
AMP + diphosphate + 6-carboxyhexanoyl-CoA
-
-
-
?
ATP + heptanedioate + CoA
?
-
-
-
-
?
ATP + heptanedioate + CoA
?
-
first enzyme of biotin biosynthesis pathway
-
-
?
ATP + heptanedioate + CoA
?
-
-
-
-
?
ATP + heptanedioate + CoA
?
-
first enzyme of biotin biosynthesis pathway
-
-
?
ATP + heptanedioate + CoA
?
Lavandula vera
-
first enzyme of biotin biosynthesis pathway
-
-
?
ATP + heptanedioate + CoA
?
-
first enzyme of biotin biosynthesis pathway
-
-
?
ATP + heptanedioate + CoA
?
-
the heptanedioyl-CoA formed in the peroxisomes is directly degraded to acetyl-CoA and malonyl-CoA by the beta-oxidation pathway
-
-
?
ATP + heptanedioate + CoA
?
-
enzyme is responsible for the first step in biotin biosynthesis by microorganisms
-
-
?
ATP + heptanedioate + CoA
?
-
enzyme is responsible for the first step in biotin biosynthesis by microorganisms
-
-
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
first enzyme of biotin biosynthesis pathway
-
?
ATP + heptanedioate + CoA
AMP + diphosphate + heptanedioyl-CoA
first enzyme of biotin biosynthesis pathway
-
?
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evolution
Aquifex aeolicus BioW represents a distinct protein fold within the superfamily of adenylating enzymes
evolution
the biotin pathway genes responsible for pimelate moiety synthesis vary widely among bacteria whereas the ring synthesis genes are highly conserved. 6-Carboxyhexanoate-CoA ligase is essential in Bacillus subtilis, encoded by gene bioW, while it is not in Escherchia coli
evolution
-
the biotin pathway genes responsible for pimelate moiety synthesis vary widely among bacteria whereas the ring synthesis genes are highly conserved. 6-Carboxyhexanoate-CoA ligase is essential in Bacillus subtilis, encoded by gene bioW, while it is not in Escherchia coli
-
malfunction
BioW activity to hydrolyze adenylates of noncognate substrates can be abolished by mutation of a single residue, R159A
malfunction
deletion of bioW causes a biotin auxotrophic phenotype whereas deletion of bioI does not. Growth phenotypes of Bacillus subtilis bioW and bioI mutant strains, biotin auxotrophy due to bioW inactivation, overview
malfunction
-
deletion of bioW causes a biotin auxotrophic phenotype whereas deletion of bioI does not. Growth phenotypes of Bacillus subtilis bioW and bioI mutant strains, biotin auxotrophy due to bioW inactivation, overview
-
metabolism
the enzyme catalyzes the first committed step of biotin biosynthesis, overview. The biotin pathway genes responsible for pimelate moiety synthesis vary widely among bacteria whereas the ring synthesis genes are highly conserved. Bacillus subtilis seems to have redundant genes, bioI and bioW, for generation of the pimelate intermediate. Pimelic acid originating from fatty acid synthesis pathway is a bona fide precursor of biotin in Bacillus subtilis. Synthesis of pimelate depends on fatty acid synthesis in Bacillus subtilis
metabolism
-
the enzyme catalyzes the first committed step of biotin biosynthesis, overview. The biotin pathway genes responsible for pimelate moiety synthesis vary widely among bacteria whereas the ring synthesis genes are highly conserved. Bacillus subtilis seems to have redundant genes, bioI and bioW, for generation of the pimelate intermediate. Pimelic acid originating from fatty acid synthesis pathway is a bona fide precursor of biotin in Bacillus subtilis. Synthesis of pimelate depends on fatty acid synthesis in Bacillus subtilis
-
physiological function
biotin is an essential vitamin in plants and mammals, functioning as the carbon dioxide carrier within central lipid metabolism. Bacterial pimeloyl-CoA synthetase (BioW) acts as a highly specific substrate-selection gate, ensuring the integrity of the carbon chain in biotin synthesis. BioW catalyzes the condensation of pimelic acid (C7 dicarboxylic acid) with CoASH in an ATP-dependent manner to form pimeloyl-CoA, the first dedicated biotin building block
physiological function
BioW is a pimeloyl-CoA synthetase that converts pimelic acid to pimeloyl-CoA. The essentiality of BioW for biotin synthesis indicates that the free form of pimelic acid is an intermediate in biotin synthesis. Bacillus subtilis has redundant genes, bioI and bioW, for generation of the pimelate intermediate. Expression of either Bacillus subtilis BioW or BioI bypasses the biotin auxotrophy of an Escherichia coli DELTAbioC DELTAbioH mutant strain SLT25
physiological function
-
BioW is a pimeloyl-CoA synthetase that converts pimelic acid to pimeloyl-CoA. The essentiality of BioW for biotin synthesis indicates that the free form of pimelic acid is an intermediate in biotin synthesis. Bacillus subtilis has redundant genes, bioI and bioW, for generation of the pimelate intermediate. Expression of either Bacillus subtilis BioW or BioI bypasses the biotin auxotrophy of an Escherichia coli DELTAbioC DELTAbioH mutant strain SLT25
-
physiological function
-
biotin is an essential vitamin in plants and mammals, functioning as the carbon dioxide carrier within central lipid metabolism. Bacterial pimeloyl-CoA synthetase (BioW) acts as a highly specific substrate-selection gate, ensuring the integrity of the carbon chain in biotin synthesis. BioW catalyzes the condensation of pimelic acid (C7 dicarboxylic acid) with CoASH in an ATP-dependent manner to form pimeloyl-CoA, the first dedicated biotin building block
-
additional information
residues controlling substrate binding and catalysis include Tyr199, Tyr211, Arg213 and Arg227
additional information
-
residues controlling substrate binding and catalysis include Tyr199, Tyr211, Arg213 and Arg227
additional information
structure-function relationship
additional information
substrate-bound structures are determined to identify the enzyme active site and elucidate the mechanistic strategy for conjugating CoA to the seven-carbon alpha,omega-dicarboxylate pimelate, a biotin precursor. Proper position of reactive groups for the two half-reactions is achieved solely through movements of active site residues as confirmed by site-directed mutational analysis. The ability of BioW to hydrolyze adenylates of noncognate substrates is reminiscent of pre-transfer proofreading observed in some tRNA synthetases. BioW can carry out three different biologically prevalent chemical reactions (adenylation, thioesterification, and proofreading) in the context of another protein fold. The movement of Arg159, which serves to position this residue to assist in thioester formation, is reminiscent of the domain movement in acetyl-CoA synthetase that positions a catalytic lysine important for adenylation away from the active site to facilitate thioester formation
additional information
-
substrate-bound structures are determined to identify the enzyme active site and elucidate the mechanistic strategy for conjugating CoA to the seven-carbon alpha,omega-dicarboxylate pimelate, a biotin precursor. Proper position of reactive groups for the two half-reactions is achieved solely through movements of active site residues as confirmed by site-directed mutational analysis. The ability of BioW to hydrolyze adenylates of noncognate substrates is reminiscent of pre-transfer proofreading observed in some tRNA synthetases. BioW can carry out three different biologically prevalent chemical reactions (adenylation, thioesterification, and proofreading) in the context of another protein fold. The movement of Arg159, which serves to position this residue to assist in thioester formation, is reminiscent of the domain movement in acetyl-CoA synthetase that positions a catalytic lysine important for adenylation away from the active site to facilitate thioester formation
additional information
-
residues controlling substrate binding and catalysis include Tyr199, Tyr211, Arg213 and Arg227
-
additional information
-
structure-function relationship
-
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H16A
site-directed mutagenesis, the mutant variant displays only a modest 20% loss in activity relative to the wild-type, reflecting the importance of these other interacting residues in stabilizing CoA binding
R159A
site-directed mutagenesis, the activity to hydrolyze adenylates of noncognate substrates is abolished in the mutant. The R159A variant can no longer proofread, but the enzyme still retains ligase activity and can catalyze the formation of pimeloyl-CoA, the mutant demonstrates a notable reduction in turnover, which is in line with the function of the residue in forming the exterior wall of the pimelate-binding cavity
R201A
site-directed mutagenesis, the mutation has little effect on product formation
R215A
site-directed mutagenesis, the mutant demonstrates a substantial reduction in product formation
S182A
site-directed mutagenesis, the mutant demonstrates a substantial reduction in product formation
Y187A
site-directed mutagenesis, the mutant demonstrates a notable reduction in turnover, which is in line with the function of the residue in forming the exterior wall of the pimelate-binding cavity
Y199A
site-directed mutagenesis, the mutation has little effect on product formation
R213A
site-directed mutagenesis, almost inactive mutant
R227E
site-directed mutagenesis, the mutant shows a turnover with the natural substrate pimelic acid that is reduced by around 25fold to about 4% activity remaining compared to the wild-type
R227K
site-directed mutagenesis, the mutant shows a turnover with the natural substrate pimelic acid that is reduced by around 25fold to about 4% activity remaining compared to the wild-type
Y199F
site-directed mutagenesis, the mutant retains 55% activity compared to wild-type, the Y199F mutant is inactive with heptanoic acid and octanoic acid, the Y199F mutant displayed a twofold greater activity with pimelic acid but no improvement with azelaic acid compared to wild-type
R213A
-
site-directed mutagenesis, almost inactive mutant
-
Y199F
-
site-directed mutagenesis, the mutant retains 55% activity compared to wild-type, the Y199F mutant is inactive with heptanoic acid and octanoic acid, the Y199F mutant displayed a twofold greater activity with pimelic acid but no improvement with azelaic acid compared to wild-type
-
Y211F
site-directed mutagenesis, almost inactive mutant
Y211F
site-directed mutagenesis, the mutant displays activity with both monocarboxylic acid substrates, heptanoic acid and octanoic acid, the Y211F mutant displays about 4fold increased activity with the suberic acid substrate and 3fold increased activity with the azelaic acid substrate relative to the wild-type BioW. The mutant enzymes is also active with 7-bromoheptanoic acid, 7-aminoheptanoic acid, 6-methylheptanoic acid, 7-phenylheptanoic acid, and 7-octenoic acid, but not with 7-aminoheptanoic acid
Y211F
site-directed mutagenesis, the mutant retains 36% activity compared to wild-type
Y211F
-
site-directed mutagenesis, almost inactive mutant
-
Y211F
-
site-directed mutagenesis, the mutant displays activity with both monocarboxylic acid substrates, heptanoic acid and octanoic acid, the Y211F mutant displays about 4fold increased activity with the suberic acid substrate and 3fold increased activity with the azelaic acid substrate relative to the wild-type BioW. The mutant enzymes is also active with 7-bromoheptanoic acid, 7-aminoheptanoic acid, 6-methylheptanoic acid, 7-phenylheptanoic acid, and 7-octenoic acid, but not with 7-aminoheptanoic acid
-
Y211F
-
site-directed mutagenesis, the mutant retains 36% activity compared to wild-type
-
additional information
deletion of the chromosomal bioW through single crossover recombination by integration of recombinant vector pMUTIN4 blocks growth in biotin-free minimal media, growth phenotypes of Bacillus subtilis bioW and bioI mutant strains, overview. Expression of bioW from the Phyper-spank promoter of vector pDR111 inserted at an ectopic site (the amyE locus) restores growth only when promoter activity is induced with IPTG, biotin auxotrophy due to bioW inactivation. Bacillus subtilis strain BI274 has an engineered bio operon driven by a phage SP01 promoter resulting in overproduction of biotin
additional information
-
deletion of the chromosomal bioW through single crossover recombination by integration of recombinant vector pMUTIN4 blocks growth in biotin-free minimal media, growth phenotypes of Bacillus subtilis bioW and bioI mutant strains, overview. Expression of bioW from the Phyper-spank promoter of vector pDR111 inserted at an ectopic site (the amyE locus) restores growth only when promoter activity is induced with IPTG, biotin auxotrophy due to bioW inactivation. Bacillus subtilis strain BI274 has an engineered bio operon driven by a phage SP01 promoter resulting in overproduction of biotin
additional information
-
deletion of the chromosomal bioW through single crossover recombination by integration of recombinant vector pMUTIN4 blocks growth in biotin-free minimal media, growth phenotypes of Bacillus subtilis bioW and bioI mutant strains, overview. Expression of bioW from the Phyper-spank promoter of vector pDR111 inserted at an ectopic site (the amyE locus) restores growth only when promoter activity is induced with IPTG, biotin auxotrophy due to bioW inactivation. Bacillus subtilis strain BI274 has an engineered bio operon driven by a phage SP01 promoter resulting in overproduction of biotin
-
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Izumi, Y.; Morita, H.; Sato, K.; Tani, Y.; Ogata, K.
Synthesis of biotin-vitamers from pimelic acid and coenzyme A by cell-free extracts of various bacteria
Biochim. Biophys. Acta
264
210-213
1972
Enterobacter cloacae, Priestia megaterium, Bacillus subtilis, Lysinibacillus sphaericus, Kocuria rosea, Pseudomonas fluorescens, Enterobacter cloacae IAM 1221, Pseudomonas fluorescens AKU 0821, Priestia megaterium NIHB 12, Kocuria rosea IFO 3764, Lysinibacillus sphaericus IFO 3525, Bacillus subtilis IAM 1193
brenda
Izumi, Y.; Morita, H.; Tani, Y.; Ogata, K.
The pimelyl-CoA synthetase responsible for the first step in biotin biosynthesis by microorganisms
Agric. Biol. Chem.
38
2257-2262
1974
Klebsiella aerogenes, Enterobacter cloacae, Priestia megaterium, Bacillus subtilis, Lysinibacillus sphaericus, Escherichia coli, Kocuria rosea, Pseudomonas fluorescens, Devosia riboflavina, Enterobacter cloacae IAM 1221, Pseudomonas fluorescens AKU 0821, Priestia megaterium NIHB 12, Kocuria rosea IFO 3764, Lysinibacillus sphaericus IFO 3525, Kocuria rosea IAM 1257, Bacillus subtilis IAM 1193, Devosia riboflavina IFO 3140
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brenda
Baldet, P.; Gerbling, H.; Axiotis, S.; Douce, R.
Biotin biosynthesis in higher plant cells. Identification of intermediates
Eur. J. Biochem.
217
479-485
1993
Lavandula vera
brenda
Ploux, O.; Soularue, P.; Marquet, A.; Gloeckler, R.; Lemoine, Y.
Investigation of the first step of biotin biosynthesis in Bacillus sphaericus. Purification and characterization of the pimeloyl-CoA synthetase, and uptake of pimelate
Biochem. J.
287
685-690
1992
Lysinibacillus sphaericus, Lysinibacillus sphaericus IFO 3525
brenda
Gerbling, H.; Axiotis, S.; Douce, R.
A new acyl-CoA synthetase, located in higher plant cytosol
J. Plant Physiol.
143
561-564
1994
Pisum sativum
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brenda
Bower, S.; Perkins, J.B.; Yocum, R.R.; Howitt, C.L.; Rahaim, P.; Pero, J.
Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon
J. Bacteriol.
178
4122-4130
1996
Bacillus subtilis, Bacillus subtilis IAM 1193
brenda
Binieda, A.; Fuhrmann, M.; Lehner, B.; Rey-Berthod, C.; Frutiger-Hughes, S.; Hughes, G.; Shaw, N.M.
Purification, characterization, DNA sequence and cloning of a pimeloyl-CoA synthetase from Pseudomonas mendocina 35
Biochem. J.
340
793-801
1999
Pseudomonas mendocina (Q9ZER2), Pseudomonas mendocina 35 (Q9ZER2)
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Manandhar, M.; Cronan, J.E.
Pimelic acid, the first precursor of the Bacillus subtilis biotin synthesis pathway, exists as the free acid and is assembled by fatty acid synthesis
Mol. Microbiol.
104
595-607
2017
Bacillus subtilis (P53559), Bacillus subtilis, Bacillus subtilis 168 (P53559)
brenda
Wang, M.; Moynie, L.; Harrison, P.J.; Kelly, V.; Piper, A.; Naismith, J.H.; Campopiano, D.J.
Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters
Nat. Chem. Biol.
13
660-667
2017
Bacillus subtilis (P53559), Bacillus subtilis, Bacillus subtilis 168 (P53559)
brenda
Estrada, P.; Manandhar, M.; Dong, S.H.; Deveryshetty, J.; Agarwal, V.; Cronan, J.E.; Nair, S.K.
The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes
Nat. Chem. Biol.
13
668-674
2017
Bacillus amyloliquefaciens (E1UV19), Aquifex aeolicus (O67575), Aquifex aeolicus, Bacillus amyloliquefaciens ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393 (E1UV19)
brenda