Information on EC 2.3.1.19 - phosphate butyryltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.3.1.19
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RECOMMENDED NAME
GeneOntology No.
phosphate butyryltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
butanoyl-CoA + phosphate = CoA + butanoyl phosphate
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
butanoate fermentation
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Butanoate metabolism
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Metabolic pathways
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pyruvate fermentation to butanoate
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SYSTEMATIC NAME
IUBMB Comments
butanoyl-CoA:phosphate butanoyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-01-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NCIMB 8052
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Manually annotated by BRENDA team
strain VPI 13437, identical with Clostridium butylicum NRRL B593
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Manually annotated by BRENDA team
strain VPI 13437, identical with Clostridium butylicum NRRL B593
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Manually annotated by BRENDA team
Clostridium saccharoacetobutylicum
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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The product pattern of a gene disruption mutant is altered to high ethanol, i.e. 12.1 g/l, and high butanol, i.e. 8.0 g/l, titers in fermentations with pH regulated above 5.0. Glucose fed-batch cultivation elevates the ethanol concentration to 32.4 g/l, yielding a more than fourfold increased alcohol to acetone ratio as compared to the wildtype. The mutant is still capable to take up butanoate when externally added during the late exponential growth phase. Findings suggest that alternative pathways of butanoate re-assimilation exist in Clostridium acetobutylicum
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-methyl-propionyl-CoA + phosphate
2-methylpropionylphosphate + CoA
show the reaction diagram
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-
-
?
3-hydroxybutanoyl-CoA + phosphate
3-hydroxybutanoylphosphate + CoA
show the reaction diagram
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-
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r
4-hydroxybutanoyl-CoA + phosphate
4-hydroxybutanoylphosphate + CoA
show the reaction diagram
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-
-
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r
4-hydroxypentanoyl-CoA + phosphate
4-hydroxypentanoylphosphate + CoA
show the reaction diagram
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-
-
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r
acetoacetyl-CoA + phosphate
acetoacetylphosphate + CoA
show the reaction diagram
acetyl-CoA + phosphate
acetylphosphate + CoA
show the reaction diagram
butanoyl-CoA + phosphate
butanoylphosphate + CoA
show the reaction diagram
isobutanoyl-CoA + phosphate
isobutanoylphosphate + CoA
show the reaction diagram
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30% of butanoylphosphate formation
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?
isopentanoyl-CoA + phosphate
isopentanoylphosphate + CoA
show the reaction diagram
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95% of butanoylphosphate formation
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?
n-pentanoyl-CoA + phosphate
n-pentanoylphosphate + CoA
show the reaction diagram
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78% of butanoylphosphate formation
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?
n-propionyl-CoA + phosphate
n-propionylphosphate + CoA
show the reaction diagram
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23% of butanoylphosphate formation
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
butanoyl-CoA + phosphate
butanoylphosphate + CoA
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
acetoacetyl-CoA
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3.33
acetyl-CoA
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0.04 - 0.11
Butanoyl-CoA
0.26
Butanoylphosphate
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0.14 - 12.9
phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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study on gene dosage effects
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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butanoylphosphate formation
8.8
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butanoyl-CoA formation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 9.5
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butanoylphosphate formation, less than 50% of maximal activity above and below
6.5 - 8
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butanoylphosphate formation, 50% of maximal activity at pH 6.5, 80% of maximal activity at pH 8.0
6.8 - 9.5
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butanoyl-CoA formation, less than 50% of maximal activity above and below
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
activity is maximal in the late exponential growth phase. The branched amino acids isoleucine and valine activate Ptb expression. ActBm, a sigma54 regulator from Bacillus megaterium whose gene is situated upstream from the ptb gene, activates its expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
205000
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gel filtration
264000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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8 * 31000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, less purified preparation, 50% v/v glycerol, 50% loss of activity in 5 d
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liquid N2, purified preparation, 50 mM sodium phosphate buffer, pH 7.0, various NaCl concentrations, 92-100% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the phosphotransbutyrylase promoter is used to produce butanol from butyryl-CoA with alcohol/aldehyde dehydrogenase
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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use of enzyme for in vitro biosynthesis of poly(hydroxyalkanoic acid)
synthesis
the phosphotransbutyrylase promoter is used to produce butanol from butyryl-CoA with alcohol/aldehyde dehydrogenase
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