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Information on EC 2.3.1.222 - phosphate propanoyltransferase
for references in articles please use BRENDA:EC2.3.1.222
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.222 phosphate propanoyltransferase
IUBMB Comments
Part of the degradation pathway for propane-1,2-diol .
The enzyme appears in viruses and cellular organisms
- 2.3.1.222
- propionaldehyde
- reuteri
- 3-hydroxypropionaldehyde
- propionate
- lactobacillus
- enterica
- 1,2-propanediol
-
3-hydroxypropionic
-
propanediol
-
biobased
-
microcompartment
-
biocatalytic
-
encapsulate
-
autotroph
showSynonyms
phosphotransacylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Moth_0864
Moth_1181
PduL
pduL1
pduL2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
propanoyl-CoA + phosphate = CoA + propanoyl phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
(S)-propane-1,2-diol degradation, L-threonine degradation I
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SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:phosphate propanoyltransferase
Part of the degradation pathway for propane-1,2-diol .
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CoA + butyryl phosphate
butyryl-CoA + phosphate
Substrates: -
Products: -
Products: -
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
Substrates: -
Products: -
Products: -
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
Substrates: reaction of EC 2.3.1.8
Products: -
Products: -
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
Substrates: no activity with acetyl phosphate in the reverse direction
Products: -
Products: -
ir
acetyl-CoA + phosphate
CoA + acetyl phosphate
Substrates: reaction of EC 2.3.1.8
Products: -
Products: -
ir
acetyl-CoA + phosphate
CoA + acetyl phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: -
Products: -
Products: -
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: reaction of EC 2.3.1.8
Products: -
Products: -
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: no activity with acetyl phosphate in the reverse direction
Products: -
Products: -
ir
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
Substrates: -
Products: -
Products: -
r
butanoyl-CoA + phosphate
CoA + butanoyl phosphate
Substrates: reaction of EC 2.3.1.19
Products: -
Products: -
?
butanoyl-CoA + phosphate
CoA + butanoyl phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: reaction of EC 2.3.1.19
Products: -
Products: -
?
butyryl-CoA + phosphate
CoA + butyryl phosphate
Substrates: -
Products: -
Products: -
r
butyryl-CoA + phosphate
CoA + butyryl phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: -
Products: -
Products: -
r
CoA + acetyl phosphate
acetyl-CoA + phosphate
Substrates: -
Products: -
Products: -
r
CoA + acetyl phosphate
acetyl-CoA + phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: -
Products: -
Products: -
r
CoA + acetyl phosphate
acetyl-CoA + phosphate
-
Substrates: PduL-His8 is 3.8fold more active with propionyl phosphate than with acetyl phosphate
Products: -
Products: -
r
CoA + propanoyl phosphate
propanoyl-CoA + phosphate
Substrates: -
Products: -
Products: -
r
CoA + propanoyl phosphate
propanoyl-CoA + phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: -
Products: -
Products: -
r
CoA + propanoyl phosphate
propanoyl-CoA + phosphate
-
Substrates: PduL-His8 is 3.8fold more active with propionyl phosphate than with acetyl phosphate
Products: -
Products: -
r
propanoyl-CoA + phosphate
CoA + propanoyl phosphate
Substrates: -
Products: -
Products: -
r
propanoyl-CoA + phosphate
CoA + propanoyl phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: -
Products: -
Products: -
r
propanoyl-CoA + phosphate
CoA + propanoyl phosphate
Substrates: -
Products: -
Products: -
?
propanoyl-CoA + phosphate
CoA + propanoyl phosphate
Substrates: -
Products: -
Products: -
?
propanoyl-CoA + phosphate
CoA + propanoyl phosphate
-
Substrates: -
Products: -
Products: -
r
propanoyl-CoA + phosphate
CoA + propanoyl phosphate
Substrates: -
Products: -
Products: -
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
Substrates: -
Products: -
Products: -
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
Neomoorella thermoacetica ATCC 39073
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with butyryl phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with butyryl phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: butanoyl-CoA, acetyl phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: butanoyl-CoA, acetyl phosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
propanoyl-CoA + phosphate
CoA + propanoyl phosphate
-
Substrates: -
Products: -
Products: -
r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mn2+
0.1 microM, 82% residual activity; 0.2 microM, 40% residual activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.61
propanoyl phosphate
-
reverse reaction, pH and temperature not specified in the publication
0.97
acetyl phosphate
-
reverse reaction, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20.7
propanoyl phosphate
-
reverse reaction, pH and temperature not specified in the publication
5.4
acetyl phosphate
-
reverse reaction, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
33.9
propanoyl phosphate
-
reverse reaction, pH and temperature not specified in the publication
5.6
acetyl phosphate
-
reverse reaction, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
recombinant His8-tagged PduL in soluble fraction of the expressing Escherichia coli strain BE554, pH and temperature not specified in the publication
8.9
-
wild-type strain, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Neomoorella thermoacetica ATCC 39073
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
-
PduL is a phosphotransacylase, PTAC, required for 1,2-propanediol degradation
evolution
-
PduL homologues are distributed among at least 49 bacterial species but are absent from the Archaea and Eukarya. Sequence analyses show that PduL is unrelated in amino acid sequence to known phosphotransacylase, PTAC, enzymes
evolution
the phosphotransacylase (PTAC) predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). PduL and Pta exemplify functional, but not structural, convergent evolution
evolution
the phosphotransacylase (PTAC) predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). PduL and Pta exemplify functional, but not structural, convergent evolution
evolution
-
the phosphotransacylase (PTAC) predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). PduL and Pta exemplify functional, but not structural, convergent evolution
-
malfunction
-
pduL mutants are unable to ferment 1,2-propanediol and are also impaired for aerobic growth on this compound, overview. Ectopic expression of pduL corrects the growth defects of a pta mutant, the pta gene encodes another PTAC enzyme
malfunction
both pduL genes (pduL1 and pduL2) are associated with acetate formation via acetyl-coenzyme A (acetyl-CoA). Their disruption enables a shift in the homoacetic pathway to the genetically synthesized homolactic pathway via pyruvate
malfunction
Neomoorella thermoacetica ATCC 39073
-
both pduL genes (pduL1 and pduL2) are associated with acetate formation via acetyl-coenzyme A (acetyl-CoA). Their disruption enables a shift in the homoacetic pathway to the genetically synthesized homolactic pathway via pyruvate
-
metabolism
-
PduL is required in the 1,2-propandiol degradation pathway, overview
metabolism
the fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt bacterial microcompartments(BMC)-based metabolism, while not affecting most commensal organisms that require phosphotransacylase (PTAC) activity
metabolism
both pduL genes (pduL1 and pduL2) are associated with acetate formation via acetyl-coenzyme A (acetyl-CoA). Their disruption enables a shift in the homoacetic pathway to the genetically synthesized homolactic pathway via pyruvate
metabolism
the fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt bacterial microcompartments(BMC)-based metabolism, while not affecting most commensal organisms that require phosphotransacylase (PTAC) activity
metabolism
Neomoorella thermoacetica ATCC 39073
-
both pduL genes (pduL1 and pduL2) are associated with acetate formation via acetyl-coenzyme A (acetyl-CoA). Their disruption enables a shift in the homoacetic pathway to the genetically synthesized homolactic pathway via pyruvate
-
metabolism
-
the fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt bacterial microcompartments(BMC)-based metabolism, while not affecting most commensal organisms that require phosphotransacylase (PTAC) activity
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are obtained from sitting drop experiments at 22°C. High-resolution PduL crystal structures with bound substrates. The PduL fold is unrelated to that of Pta. It contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping phosphotransacylase (PTAC)
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His8-tagged PduL from Escherichia coli strain BE554 soluble fraction by nickel affinity chromatographhy
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
gene pduL, DNA and amino acid sequence determination and analysis, sequence comparison, expression as His8-tagged protein in Escherichia coli strain BE554 mostly in inclusion bodies
-
expression in Escherichia coli BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, Y.; Leal, N.A.; Sampson, E.M.; Johnson, C.L.; Havemann, G.D.; Bobik, T.A.
PduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar typhimurium LT2
J. Bacteriol.
189
1589-1596
2007
Salmonella enterica, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Iwasaki, Y.; Kita, A.; Yoshida, K.; Tajima, T.; Yano, S.; Shou, T.; Saito, M.; Kato, J.; Murakami, K.; Nakashimada, Y.
Homolactic acid fermentation by the genetically engineered thermophilic homoacetogen Moorella thermoacetica ATCC 39073
Appl. Environ. Microbiol.
83
e00247-17
2017
Neomoorella thermoacetica (Q2RK58), Neomoorella thermoacetica (Q2RJ94), Neomoorella thermoacetica ATCC 39073 (Q2RK58), Neomoorella thermoacetica ATCC 39073 (Q2RJ94)
brenda
Breitkopf, R.; Uhlig, R.; Drenckhan, T.; Fischer, R.J.
Two propanediol utilization-like proteins of Moorella thermoacetica with phosphotransacetylase activity
Extremophiles
20
653-661
2016
Neomoorella thermoacetica (Q2RK58), Neomoorella thermoacetica (Q2RJ94), Neomoorella thermoacetica ATCC 39073 (Q2RK58), Neomoorella thermoacetica ATCC 39073 (Q2RJ94)
brenda
Erbilgin, O.; Sutter, M.; Kerfeld, C.A.
The structural basis of coenzyme A recycling in a bacterial organelle
PLoS Biol.
14
e1002399
2016
Rhodopseudomonas palustris (Q21A54), Rhodopseudomonas palustris BisB18 (Q21A54), Salmonella enterica subsp. enterica serovar Typhimurium (Q9XDN5)
brenda
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