Information on EC 6.2.1.17 - propionate-CoA ligase

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

EC NUMBER
COMMENTARY hide
6.2.1.17
-
RECOMMENDED NAME
GeneOntology No.
propionate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + propanoate + CoA = AMP + diphosphate + propanoyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-methylcitrate cycle I
-
-
2-methylcitrate cycle II
-
-
beta-alanine biosynthesis II
-
-
L-isoleucine biosynthesis IV
-
-
Metabolic pathways
-
-
Propanoate metabolism
-
-
alanine metabolism
-
-
isoleucine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
propanoate:CoA ligase (AMP-forming)
Propenoate can act instead of propanoate. Not identical with EC 6.2.1.1 (acetate---CoA ligase) or EC 6.2.1.2 (butyrate---CoA ligase).
CAS REGISTRY NUMBER
COMMENTARY hide
150386-10-0
-
55326-49-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain OK-70-fl, DSM 636
Uniprot
Manually annotated by BRENDA team
strain OK-70-fl, DSM 636
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PNKb1
-
-
Manually annotated by BRENDA team
strain PNKb1
-
-
Manually annotated by BRENDA team
strain LT2
-
-
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 + 3-hydroxypropanoate + CoA
AMP + diphosphate + 3-hydroxypropanoyl-CoA
show the reaction diagram
ATP + 3-hydroxypropionate + CoA + NADPH
AMP + diphosphate + NADP+ + propionyl-CoA
show the reaction diagram
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
show the reaction diagram
ATP + acrylate + CoA
AMP + diphosphate + acryloyl-CoA
show the reaction diagram
ATP + acrylate + CoA
AMP + diphosphate + acrylyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acrylate + CoA + NADPH
AMP + diphosphate + NADP+ + propionyl-CoA
show the reaction diagram
same activity as with 3-hydroxypropionate
-
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
ATP + crotonate + CoA
AMP + diphosphate + crotonyl-CoA
show the reaction diagram
ATP + fumarate + CoA
AMP + diphosphate + fumaroyl-CoA
show the reaction diagram
-
14% of the activity relative to propanoate
-
-
-
ATP + glycine + CoA
?
show the reaction diagram
-
very poor substrate
-
-
?
ATP + glyoxalate + CoA
?
show the reaction diagram
-
poor substrate
-
-
?
ATP + mercaptoacetoacetate + CoA
AMP + diphosphate + mercaptoacetoacetyl-CoA
show the reaction diagram
-
very good substrate
-
-
?
ATP + propanoate + CoA
?
show the reaction diagram
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
show the reaction diagram
ATP + salicylate + CoA
AMP + diphosphate + salicyl-CoA
show the reaction diagram
-
8% of the activity relative to propanoate
-
-
-
GTP + 3-hydroxypropionate + CoA + NADPH
GMP + diphosphate + NADP+ + propionyl-CoA
show the reaction diagram
24% of activity
-
-
?
UTP + 3-hydroxypropionate + CoA + NADPH
UMP + diphosphate + NADP+ + propionyl-CoA
show the reaction diagram
20% of activity
-
-
?
additional information
?
-
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 + 3-hydroxypropanoate + CoA
AMP + diphosphate + 3-hydroxypropanoyl-CoA
show the reaction diagram
ATP + 3-hydroxypropionate + CoA + NADPH
AMP + diphosphate + NADP+ + propionyl-CoA
show the reaction diagram
Q8VRG6
involved in CO2 fixation via 3-hydroxypropionate cycle
-
-
?
ATP + propanoate + CoA
?
show the reaction diagram
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
show the reaction diagram
additional information
?
-
-
activates volatile fatty acids
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cs+
can partially substitute for K+
K+
required, half aximal activity at 4 mM
NH4+
can partially substitute for K+
Rb+
can partially substitute for K+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-nitrobenzoate
-
inhibition of propanoyl-CoA formation in solubilized mitochondria
adenosine 5'-propyl phosphate
-
strong inhibition, bi uni uni bi ping pong mechanism
ATP
-
substrate inhibition at high concentrations, above 20 mM for the liver enzyme and above 10 mM for the mammary gland enzyme
Butyrate
dithiothreitol
-
5 or 10 mM
GSH
-
5 or 20 mM
MgCl2
-
above 10 mM
Octanoate
propanoate
-
inhibits acetate activation and butyrate activation
propyl-AMP
-
competitive with ATP and propionyl-AMP, mixed type inhibition with propionate, uncompetitive with CoA
salicylate
-
inhibition of propanoyl-CoA formation in solubilized mitochondria
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 0.19
3-hydroxypropanoate
0.015
3-hydroxypropionate
pH 7.8, 55C
1.7 - 32
acetate
0.279 - 1.42
Acrylate
0.045 - 4.8
ATP
4.6 - 82
Butyrate
0.01 - 1
CoA
0.254
diphosphate
-
pH 7.5, 37C
0.01
NADPH
pH 7.8, 55C
0.12 - 5.3
propanoate
0.02 - 0.26
propionate
0.023
propionyl-AMP
-
pH 7.5, 37C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8 - 23
3-hydroxypropanoate
12
3-hydroxypropionate
Chloroflexus aurantiacus
Q8VRG6
pH 7.8, 55C
4.8 - 32
acetate
1.1 - 26
Acrylate
1.1 - 34
ATP
0.87 - 6
Butyrate
1 - 42
CoA
79
diphosphate
Salmonella enterica
-
pH 7.5, 37C
5.6
propanoate
Metallosphaera sedula
A4YGR1
pH 8.4, 45C, coupled spectrophotometric assay
1.2 - 33
propionate
78
propionyl-AMP
Salmonella enterica
-
pH 7.5, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00002
propyl-AMP
-
competitive with ATP, pH 7.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
heterotrophic grown cells
0.06
-
native enzyme with glycine as substrate, pH 7.5, 37C
0.091
autotrophic grown cells
0.3
-
pH 7.5, 37C, with acetate as substrate
0.325
-
-
0.63
-
pH 7.5, 37C, with propanoate as substrate
0.65
-
native enzyme with glyoxalate as substrate, pH 7.5, 37C
2.5
purified enzyme, pH 7.8, 55C
3.36
-
-
6.7
-
purified recombinant enzyme
22
-
native enzyme with propionate as substrate, pH 7.5, 37C
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
cow liver enzyme
7.5
-
assay at
8 - 9
-
mammary gland enzyme, cow
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
cow liver enzyme
50
-
mammary gland enzyme, cow
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
-
at 25C the activity is 55% of that at 37C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
of midlactation cow, no activity in calf
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
2 * 35000, SDS-PAGE
68700
-
x * 68700, estimated from SDS-PAGE
70900
-
calculated from amino acid sequence
71300
-
calculated from amino acid sequence
73400
-
sucrose density gradient centrifugation
74000
-
2 * 74000
140000
-
recombinant enzyme, gel filtration
340000
gel filtration
500000 - 800000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 68700, estimated from SDS-PAGE
monomer
tetramer
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
-
cow liver enzyme
655
8.5 - 9
-
mammary gland enzyme, cow
655
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 30
-
5 min, maximal stability, cow liver and mammary gland enzymes
65
stable for at least 15 min in presence of 20% glycerol and 1 mM dithioerythreitol
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing leads to a complete loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10% glycerol, stable for months
-
-20C, 20% glycerol, 1 mM dithioerythreitol, stable for several weeks
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and mutant enzymes using chitin affinity chromatography
-
native enzyme 95fold to homogeneity by ammonium sulfate fractionation, hydrophobic interaction, anion exchange and adsorption chromatography, followed by gel filtration
partial
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant; recombinant enzyme using His-tag
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complementation studies
-
expressed in Escherichia coli ER2566
-
expressed in Escherichia coli Rosetta(DE3); expression in Escherichia coli
expressed in Escherichia coli strain BAP1
-
expressed in Escherichia coli XL1-Blue cells
-
expression of the His-tagged enzyme in Escherichia coli
-
gene prpE, expression in Escherichia coli under the control of the IPTG-inducible tac promoter PtaclacUV5
-
gene prpE, functional expression in Sorangium cellulosum So ce90 leading to a significant increase in the resolution of epothilones B/A, with an epothilone B to A ratio of 127 to 1, which is 100times higher than that of the wild-type cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G245A
-
58% of activity
G249A
-
11% of activity
K248A
-
12% of activity
K248E
-
6% of activity
K592A
-
complete loss of activity
K592E
-
complete loss of activity
P247A
-
activity almost not affected
additional information
-
coexpression of the enzyme from Salmonella enterica together with the polyhydroxyalkanoate synthesis operon phaBCA from Ralstonia eutropha in Escherichia coli to produce poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV) of specified composition between 5% and 18% HV, Metabolic pathways for PHBV synthesis, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
rapid radiochemical assay method with high sensitivity and specificity
synthesis
-
used for incorporation of unusual acyl groups into biopolymers and polyketide antibiotics
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