Information on EC 2.7.2.7 - butyrate kinase

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

EC NUMBER
COMMENTARY
2.7.2.7
-
RECOMMENDED NAME
GeneOntology No.
butyrate kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + butanoate = ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
phospho group transfer
-
-
phospho group transfer
Butyrivibrio fibrisolvens D1T, Butyrivibrio hungatei JK615T, Clostridium acetobutylicum M5, Clostridium proteoclasticum B316T
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Butanoate metabolism
-
Metabolic pathways
-
pyruvate fermentation to butanoate
-
SYSTEMATIC NAME
IUBMB Comments
ATP:butanoate 1-phosphotransferase
The enzyme from Clostridium sp. also acts, more slowly, on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14 sedoheptulokinase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
BK
-
-
-
-
Buk
-
-
-
-
Buk2
Q9X278
-
butyrate kinase
-
-
butyrate kinase
Butyrivibrio fibrisolvens D1T
-
-
-
butyrate kinase
-
-
butyrate kinase
Butyrivibrio hungatei JK615T
-
-
-
butyrate kinase
Clostridium acetobutylicum M5
-
-
-
butyrate kinase
-
-
butyrate kinase
Clostridium proteoclasticum B316T
-
-
-
butyrate kinase
-
-
butyrate kinase 2
-
-
butyrate kinase 2
Q9X278
-
butyrate kinase I
-
isozyme
butyrate kinase II
-
isozyme
butyrokinase
-
-
-
-
kinase (phosphorylating), butyrate
-
-
-
-
kinase, butyrate (phosphorylating)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37278-14-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain D1T (ATCC 19171)
-
-
Manually annotated by BRENDA team
Butyrivibrio fibrisolvens D1T
strain D1T (ATCC 19171)
-
-
Manually annotated by BRENDA team
Butyrivibrio hungatei JK615T
strain JK615T
-
-
Manually annotated by BRENDA team
; expression in Escherichia coli, which expresses the non-natural BPEC pathway consisting of butyrate kinase and phosphotransbutyrylase from Clostridium acetobutylicum and PHA synthase from Thiococcus pfennigii with and without PhaP1 from Ralstonia eutropha H16
-
-
Manually annotated by BRENDA team
strain M5, loss of the pSOL1 megaplasmid, complemented with aad expressed from the phosphotransbutyrylase promoter
-
-
Manually annotated by BRENDA team
Clostridium acetobutylicum M5
strain M5, loss of the pSOL1 megaplasmid, complemented with aad expressed from the phosphotransbutyrylase promoter
-
-
Manually annotated by BRENDA team
Clostridium proteoclasticum B316T
strain B316T
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
-
poor substrate
-
-
?
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
-
6% of the activity with butanoate
-
-
?
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
-
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
r
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
-
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
r
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
Q9X278
-
-
-
r
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
Q9X278
-
-
-
r
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
-
50% of the activity with butanoate
-
-
?
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
-
54% of the activity with butanoate
-
-
?
ATP + isovalerate
ADP + isopentanoyl phosphate
show the reaction diagram
-
32% of the activity with butanoate
-
-
?
ATP + propionate
ADP + propanoyl phosphate
show the reaction diagram
-
-
-
-
-
ATP + propionate
ADP + propanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + propionate
ADP + propanoyl phosphate
show the reaction diagram
-
as active as butanoate
-
-
?
ATP + propionate
ADP + propanoyl phosphate
show the reaction diagram
-
43% of the activity with butanoate
-
-
?
ATP + valerate
ADP + pentanoyl phosphate
show the reaction diagram
-
-
-
-
-
ATP + valerate
ADP + pentanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + valerate
ADP + pentanoyl phosphate
show the reaction diagram
-
12% of the activity with butanoate
-
-
?
ATP + valerate
ADP + pentanoyl phosphate
show the reaction diagram
-
89% of the activity with butanoate
-
-
?
ATP + vinyl acetate
ADP + vinylacetyl phosphate
show the reaction diagram
-
23% of the activity with butanoate
-
-
?
additional information
?
-
-
enzyme is involved in production of butyrate
-
-
-
additional information
?
-
-
the enzyme is not regulated by the end-product, its specific activity is constant during the fermentation
-
-
-
additional information
?
-
-
semi-automated reverse engineering algorithm. The reconstructed metabolic network was used to create a genome-scale model that correctly characterized the butyrate kinase knock-out and the asolventogenic M5 pSOL1 megaplasmid degenerate strains. Systematic gene knock-out simulations performed to identify a set of genes encoding clostridial enzymes essential for growth in silico.
-
-
-
additional information
?
-
-
overexpressed PhaP1 from Ralstonia eutropha H16 affected poly(3-mercaptopropionate) [poly(3MP)] and poly(3-hydroxybutyrate) [poly(3HB)] accumulation in recombinant Escherichia coli, which expresses the non-natural BPEC pathway consisting of butyrate kinase and phosphotransbutyrylase from Clostridium acetobutylicum and PHA synthase from Thiococcus pfennigii
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
Q9X278
-
-
-
r
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
Q9X278
-
-
-
r
additional information
?
-
-
enzyme is involved in production of butyrate
-
-
-
additional information
?
-
-
the enzyme is not regulated by the end-product, its specific activity is constant during the fermentation
-
-
-
additional information
?
-
-
semi-automated reverse engineering algorithm. The reconstructed metabolic network was used to create a genome-scale model that correctly characterized the butyrate kinase knock-out and the asolventogenic M5 pSOL1 megaplasmid degenerate strains. Systematic gene knock-out simulations performed to identify a set of genes encoding clostridial enzymes essential for growth in silico.
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
slight activation
Fe2+
-
slight activation
Mg2+
-
cation requirement is satisfied by Mn2+ or Mg2+
Mg2+
-
divalent cation requirement is satisfied by Mg2+
Mn2+
-
cation requirement is satisfied by Mn2+ or Mg2+. Km-value for Mn2+ is 27 mM
Zn2+
-
slight activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
HgCl2
-
10 mM, 47% inhibition
iodoacetamide
-
20 mM; 49% inhibition
PCMB
-
0.1 mM, 66% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
DTT
-
presence of a reducing agent is required
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.4
-
ATP
-
pH 7.2, 30C
4.23
-
ATP
-
pH 7.5, 30C, reaction with butanoate, activation with 6 mM MgSO4
5.06
-
ATP
-
pH 7.5, 30C, reaction with butanoate, activation with 6 mM MnSO4
10.8
-
Butanoate
-
pH 7.5, 30C, activation with 10 mM MgSO4
14
-
Butanoate
-
pH 7.6
14.3
-
Butanoate
-
pH 7.5, 30C, activation with 6 mM MnSO4
20
-
Butanoate
-
pH 7.2, 30C
9
-
Isobutanoate
-
pH 7.2, 30C
26
-
Propionate
-
pH 7.2, 30C
14
-
valerate
-
pH 7.6
15.3
-
valerate
-
pH 7.5, 30C, activation with 6 mM MnSO4
15.5
-
valerate
-
pH 7.5, 30C, activation with 10 mM MgSO4
77
-
Isobutanoate
-
pH 7.5, 30C, activation with 10 mM MgSO4
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.058
-
-
activity in cell-free extract
additional information
-
-
significantly lower butyrate kinase activity compared to the vaccenic acid-producing group 2 and stearic acid-producing group
additional information
-
-
high butyrate kinase activity
additional information
-
-
butyrate kinase activity lower than 40 U per mg protein; significantly lower butyrate kinase activity compared to the SA-group and the VA2-group
additional information
-
-
butyrate kinase activity more than 600 U per mg protein; high butyrate kinase activity
additional information
-
-
high butyrate kinase activity
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
8.3
-
activation by Mg2+
7.5
7.6
-
activation by Mn2+
7.5
-
-
formation of butanoyl phosphate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
10
-
pH 6: about 25% of maximal activity, pH 10.0: about 50% of maximal activity
6.5
7.8
-
pH 6.5: about 60% of maximal activity pH 7.8: about 65% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
5.9
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
isolated from the rumen of cattle and sheep
Manually annotated by BRENDA team
additional information
-
isolated from the feces human
Manually annotated by BRENDA team
additional information
Butyrivibrio fibrisolvens D1T, Butyrivibrio hungatei JK615T, Clostridium proteoclasticum B316T
-
isolated from the rumen of cattle and sheep
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
large-granule fraction and small-granule fraction
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42000
-
-
SDS-PAGE
80000
-
-
gel filtration
85000
-
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 39000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
octamer
Q9X278
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Buk2 complexed with (beta,gamma-methylene) adenosine 5'-triphosphate, sitting drop vapor diffusion method, using 1.7-3.0 M sodium formate, 1 M acetic acid (pH 4.5)
-
sitting drop vapor diffusion method, using 77 mM phosphate-citrate and 55% (w/v) PEG 200
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9.5
-
very stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
20 min, 70% loss of activity in absence of 100 mM butanoate, complete protection against inactivation in presence of mM potassium butanoate
60
-
-
1 min, complete loss of activity in absence of butanoate
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 25 mM Tris-HCl, pH 7.6, 1 mM DTT, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nickel affinity column chromatography
-
ammonium sulfate precipitiation, heparin column chromatography, and Sephadex G25 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression of the BPEC pathway consisting of butyrate kinase and phosphotransbutyrylase from Clostridium acetobutylicum and PHA synthase from Thiococcus pfennigii in Escherichia coli with and without phaP1 from Ralstonia eutropha H16
-
expressed in Escherichia coli B834 cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E332D
-
the mutant shows 3.82% of wild type butyrate kinase II activity
E332L
-
the mutant shows 0.34% of wild type butyrate kinase II activity
E332Q
-
the mutant shows 3.02% of wild type butyrate kinase II activity
E334D
-
the mutant shows 0.29% of wild type butyrate kinase II activity
E334L
-
the mutant shows0.58% of wild type butyrate kinase II activity
E334Q
-
the mutant shows 0.41% of wild type butyrate kinase II activity
H155L
-
the mutant shows no butyrate kinase II activity
H155Q
-
the mutant shows no butyrate kinase II activity
H183L
-
the mutant shows 0.06% of wild type butyrate kinase II activity
R150F
-
the mutant shows no butyrate kinase II activity
R150K
-
the mutant shows 21% of wild type butyrate kinase II activity
R215F E332D
-
the mutant shows 0.38% of wild type butyrate kinase II activity
H183Q
-
the mutant shows 0.19% of wild type butyrate kinase II activity
additional information
-
semi-automated reverse engineering algorithm. The reconstructed metabolic network was used to create a genome-scale model that correctly characterized the butyrate kinase knock-out and the asolventogenic M5 pSOL1 megaplasmid degenerate strains. Systematic gene knock-out simulations performed to identify a set of genes encoding clostridial enzymes essential for growth in silico.
additional information
-
metabolic engineering studies of Clostridium acetobutylicum strain M5 to produce butanol without acetone
R215K
-
the mutant shows 0.44% of wild type butyrate kinase II activity
additional information
Clostridium acetobutylicum M5
-
metabolic engineering studies of Clostridium acetobutylicum strain M5 to produce butanol without acetone
-
additional information
-
pta-deleted mutant, BK activity increases by 44%, ack-deleted mutant, similar activity as wild-type
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
optimization for biotechnological production of polyhydroxyalkanoic acids and polythioethers
synthesis
-
butanoate kinase and phosphotransbutyrylase are successfully exploited for in vitro synthesis of 3-hydroxybutyryl-CoA, 4-hydroxybutyryl-CoA, 4-hydroxyvaleryl-CoA and poly(hydroxyalkanoic acid). Combination of butanoate kinase, phosphotransbutyrylase and poly(hydroxyalkanoic acid) synthase of Chromatium vinosum establishes a new system for in vitro synthesis of poly(3-hydroxybutyric acid)
industry
Clostridium acetobutylicum M5
-
development of biologically based chemicals and fuels
-
nutrition
-
Enterococcus durans can be developed into a useful probiotic aimed at the treatment of patients suffering from ulcerative colitis
industry
-
development of biologically based chemicals and fuels
additional information
-
coexpression of PhaP1 alongside the BPEC pathway is important for optimizing strains towards enhanced polyhydroxyalkanoic acid or polythioester production