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 hide
2.7.2.7
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RECOMMENDED NAME
GeneOntology No.
butyrate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + butanoate = ADP + butanoyl phosphate
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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
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).
CAS REGISTRY NUMBER
COMMENTARY hide
37278-14-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain D1T (ATCC 19171)
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-
Manually annotated by BRENDA team
strain D1T (ATCC 19171)
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-
Manually annotated by BRENDA team
strain JK615T
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-
Manually annotated by BRENDA team
strain JK615T
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-
Manually annotated by BRENDA team
strain B316T
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-
Manually annotated by BRENDA team
strain B316T
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-
Manually annotated by BRENDA team
strain M5, loss of the pSOL1 megaplasmid, complemented with aad expressed from the phosphotransbutyrylase promoter
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
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 + valerate
ADP + pentanoyl phosphate
show the reaction diagram
ATP + vinyl acetate
ADP + vinylacetyl phosphate
show the reaction diagram
-
23% of the activity with butanoate
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-
?
additional information
?
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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
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
slight activation
Fe2+
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slight activation
Zn2+
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slight activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HgCl2
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10 mM, 47% inhibition
iodoacetamide
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20 mM; 49% inhibition
PCMB
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0.1 mM, 66% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
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presence of a reducing agent is required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4 - 5.06
ATP
10.8 - 20
Butanoate
9 - 77
Isobutanoate
26
Propionate
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pH 7.2, 30C
14 - 15.5
valerate
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Clostridium acetobutylicum
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.058
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activity in cell-free extract
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8.3
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activation by Mg2+
7.5
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formation of butanoyl phosphate
7.5 - 7.6
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activation by Mn2+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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pH 6: about 25% of maximal activity, pH 10.0: about 50% of maximal activity
6.5 - 7.8
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pH 6.5: about 60% of maximal activity pH 7.8: about 65% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 5.9
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
large-granule fraction and small-granule fraction
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
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gel filtration
85000
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non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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)
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sitting drop vapor diffusion method, using 77 mM phosphate-citrate and 55% (w/v) PEG 200
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
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very stable
642344
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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20 min, 70% loss of activity in absence of 100 mM butanoate, complete protection against inactivation in presence of mM potassium butanoate
60
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1 min, complete loss of activity in absence of butanoate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 25 mM Tris-HCl, pH 7.6, 1 mM DTT, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitiation, heparin column chromatography, and Sephadex G25 gel filtration
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nickel affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834 cells
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expression in Escherichia coli
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E332D
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the mutant shows 3.82% of wild type butyrate kinase II activity
E332L
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the mutant shows 0.34% of wild type butyrate kinase II activity
E332Q
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the mutant shows 3.02% of wild type butyrate kinase II activity
E334D
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the mutant shows 0.29% of wild type butyrate kinase II activity
E334L
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the mutant shows0.58% of wild type butyrate kinase II activity
E334Q
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the mutant shows 0.41% of wild type butyrate kinase II activity
H155L
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the mutant shows no butyrate kinase II activity
H155Q
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the mutant shows no butyrate kinase II activity
H183L
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the mutant shows 0.06% of wild type butyrate kinase II activity
H183Q
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the mutant shows 0.19% of wild type butyrate kinase II activity
R150F
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the mutant shows no butyrate kinase II activity
R150K
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the mutant shows 21% of wild type butyrate kinase II activity
R215F E332D
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the mutant shows 0.38% of wild type butyrate kinase II activity
R215K
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the mutant shows 0.44% of wild type butyrate kinase II activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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optimization for biotechnological production of polyhydroxyalkanoic acids and polythioethers
industry
nutrition
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Enterococcus durans can be developed into a useful probiotic aimed at the treatment of patients suffering from ulcerative colitis
synthesis
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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)
additional information
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coexpression of PhaP1 alongside the BPEC pathway is important for optimizing strains towards enhanced polyhydroxyalkanoic acid or polythioester production
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