Information on EC 2.7.2.15 - propionate kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.2.15
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RECOMMENDED NAME
GeneOntology No.
propionate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetate = ADP + acetyl phosphate
show the reaction diagram
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-
-
-
ATP + propanoate = ADP + propanoyl phosphate
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-1,2-propanediol degradation
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L-threonine degradation I
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Metabolic pathways
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Propanoate metabolism
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threonine metabolism
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SYSTEMATIC NAME
IUBMB Comments
ATP:propanoate phosphotransferase
Requires Mg2+. Acetate can also act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [1]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important roles in the production of propanoate [1].
CAS REGISTRY NUMBER
COMMENTARY hide
39369-28-3
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetate + ATP
acetyl phosphate + ADP
show the reaction diagram
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
ATP + butyrate
ADP + butanoyl phosphate
show the reaction diagram
ATP + propanoate
ADP + propanoyl phosphate
show the reaction diagram
CTP + propanoate
CDP + propanoyl phosphate
show the reaction diagram
GTP + propanoate
GDP + propanoyl phosphate
show the reaction diagram
-
-
-
r
propionate + ATP
propionyl phosphate + ADP
show the reaction diagram
UTP + propanoate
UDP + propanoyl phosphate
show the reaction diagram
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
enzyme binding of nucleotide mainly involves hydrophobic interactions with the base moiety and can account for the broad biochemical specificity observed between the enzyme and nucleotides, modeling
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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
25.3 - 26.92
acetate
0.112 - 126
ATP
additional information
additional information
Michaelis-Menten kinetic analysis, the enzyme shows open and closed states consistent with inter-domain motion during catalysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
120
acetate
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
120
ATP
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
60
Butyrate
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
73
CTP
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
113
GTP
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
108
propanoate
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
81
UTP
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.7
acetate
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
47
1
ATP
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
4
1.7
Butyrate
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
462
0.31
CTP
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
60
1
GTP
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
37
43.2
propanoate
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
949
0.26
UTP
Salmonella enterica subsp. enterica serovar Typhimurium
O06961
pH 7.5, 25C
65
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
98.2
-
acetate, 25C, after overproduction of TdcD
114.7
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propionate, 25C, after overproduction of TdcD
additional information
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cell extracts enriched for the PduW or TdcD protein show levels of propionate kinase activity that were about 11 and 45 fold higher than the background
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43340
-
calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the hanging drop method, crystals of native TdcD (2.6 A resolution), TdcD-Ap4A complex in the presence of ATP (2.0 A resolution), and TdcD-Ap4A (2.4 A resolution), Ap4A is bound at the active site pocket, Ap4A is present in an extended conformation with one adenosine moiety present in the nucleotide binding site and other in the propionate binding site
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purified enzyme in complex with ATP, GTP, or CTP, soaking of crystals in 0.1 M Bis-Tris, pH 6.5, 35% pentaerythritol ethoxylate, crystals of enzyme StTdcD in complex with phosphate, AMP, ATP, Ap4, GMP, GDP, GTP, CMP and CTP are obtained using variations of crystallization conditions reported for the unliganded enzyme, X-ray diffraction structure determination and analyis at 2.4-3.0 A resolution, molecular replacement method using a polyalanine model of the unliganded StTdcD protomer, PDB ID 2E1Y as the search model, modeling
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity by Ni-NTA affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ackA gene is expressed in Escherichia coli to efficiently convert propionyl-phosphate to propionate
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cloned in pRSET C vector and overexpressed in Escherichia coli BL21(DE3)pLysS along with an N-terminal hexahistidine tag
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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in order to realise an efficient production of 1-propanol through amino acid biosynthetic pathway using glucose or glycerol as a carbon source L-threonine overproducing strain, TH20 is employed as a base strain and engineered to establish a novel pathway leading to the formation of1-propanol under aerobic condition. The engineered strain, PRO2, harbouring a plasmid overexpressing the atoDA, adhEmut, thrABC, ackA and cimA genes is able to produce more than 10 g/L of 1-propanol from glucose or glycerol in aerobic fed-batch fermentation
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