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IUBMB Comments The enzyme is most specific in Escherichia coli , where the preferred substrates are propanoyl-CoA and succinate. In other organisms, the enzyme uses acetyl-CoA at the same rate as propanoyl-CoA (cf . EC 2.8.3.18 , succinyl-CoA:acetate CoA-transferase).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms propionate:succinate coa-transferase, propionyl coa:succinate coa transferase, more
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acetate:succinate CoA-transferase
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propionate:succinate CoA-transferase
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propionyl CoA:succinate CoA transferase
propionyl-CoA transferase
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propionyl-CoA:succinyl-CoA transferase
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succinyl-CoA: propionate CoA-transferase
succinyl-CoA:propionate CoA-transferase
ASCT
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CoA transferase
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propionyl CoA:succinate CoA transferase
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propionyl CoA:succinate CoA transferase
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SCACT
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succinyl-CoA: propionate CoA-transferase
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succinyl-CoA: propionate CoA-transferase
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succinyl-CoA:propionate CoA-transferase
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succinyl-CoA:propionate CoA-transferase
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YgfH
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propanoyl-CoA + succinate = propanoate + succinyl-CoA
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MetaCyc
(S)-lactate fermentation to propanoate, acetate and hydrogen, anaerobic energy metabolism (invertebrates, mitochondrial), conversion of succinate to propanoate, pyruvate fermentation to propanoate I
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propanoyl-CoA:succinate CoA transferase
The enzyme is most specific in Escherichia coli, where the preferred substrates are propanoyl-CoA and succinate. In other organisms, the enzyme uses acetyl-CoA at the same rate as propanoyl-CoA (cf. EC 2.8.3.18, succinyl-CoA:acetate CoA-transferase).
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acetate + succinyl-CoA
acetyl-CoA + succinate
acetyl-CoA + succinate
acetate + succinyl-CoA
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Substrates: - Products: -
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propanoate + succinyl-CoA
propanoyl-CoA + succinate
propanoyl-CoA + succinate
propanoate + succinyl-CoA
additional information
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acetate + succinyl-CoA
acetyl-CoA + succinate
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Substrates: - Products: -
r
acetate + succinyl-CoA
acetyl-CoA + succinate
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Substrates: - Products: -
r
propanoate + succinyl-CoA
propanoyl-CoA + succinate
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Substrates: - Products: -
r
propanoate + succinyl-CoA
propanoyl-CoA + succinate
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Substrates: - Products: -
r
propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
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propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
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propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
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propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
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propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
r
propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
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propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
r
propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
r
additional information
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Substrates: the enzyme also catalyzes the acetate:succinate CoA-transferase reaction Products: -
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additional information
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Substrates: the enzyme can also use acetate and acetyl-CoA as substrate instead of propionate and propanoyl-CoA, respectively. The enzyme does not catalyze transfer from acetyl-CoA to methylmalonate, from beta-hydroxy-beta-methylglutaryl-CoA to acetate or from acetoacetyl-CoA to succinate Products: -
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additional information
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Substrates: the enzyme does not catalyse the transfer of CoA from succinyl-CoA to acetoacetate. The enzyme does not catalyse the transfer of CoA from acetyl-CoA to methylmalonate, acetoacetate, formate, or fluoroacetate, or from 3-hydroxy-3-methylglutaryl-CoA to acetate Products: -
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additional information
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Substrates: the enzyme can also use acetate and acetyl-CoA as substrate instead of propionate and propanoyl-CoA, respectively. The enzyme does not catalyze transfer from acetyl-CoA to methylmalonate, from beta-hydroxy-beta-methylglutaryl-CoA to acetate or from acetoacetyl-CoA to succinate Products: -
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additional information
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Substrates: the enzyme does not catalyse the transfer of CoA from succinyl-CoA to acetoacetate. The enzyme does not catalyse the transfer of CoA from acetyl-CoA to methylmalonate, acetoacetate, formate, or fluoroacetate, or from 3-hydroxy-3-methylglutaryl-CoA to acetate Products: -
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propanoyl-CoA + succinate
propanoate + succinyl-CoA
propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
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propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
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propanoyl-CoA + succinate
propanoate + succinyl-CoA
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Substrates: - Products: -
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Mg2+
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5 mM used in assay conditions
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additional information
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not activated by malate, ADP, or phosphate
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7
acetate
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with acetate as cosubstrate, at pH 8.0 and 25°C
0.0071
propanoyl-CoA
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at pH 7.0 and 25°C
0.068 - 0.13
succinyl-CoA
0.0625
propanoate
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at pH 8.0 and 25°C
0.62
propanoate
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at pH 7.8 and 25°C
0.068
succinyl-CoA
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at pH 8.0 and 25°C
0.068
succinyl-CoA
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with propanoate as cosubstrate, at pH 7.8 and 25°C
0.13
succinyl-CoA
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with acetate as cosubstrate, at pH 8.0 and 25°C
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0.72
propanoyl-CoA
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at pH 7.0 and 25°C
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100
propanoyl-CoA
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at pH 7.0 and 25°C
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0.0917
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at pH 8.0 and 25°C
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6.5 - 8
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the enzyme has a broad optimum between pH 6.5 and 8.0, 50% activity at pH 5.5. There is no enzymatic activity at pH 8.5
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brenda
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brenda
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anaerobic mitochondria
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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metabolism
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the enzyme is important in forming both acetate and propanoate
metabolism
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the enzyme is important in forming both acetate and propanoate
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APSCT_FASHE
478
0
52433
Swiss-Prot
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SCPC_ECOLI
Escherichia coli (strain K12)
492
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53824
Swiss-Prot
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x * 54106, calculated from amino acid sequence
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x * 54106, calculated from amino acid sequence
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-20°C, 0.1 M phosphate (pH 6.8) containing 0.1 mM EDTA, the enzyme is quite stable at protein concentrations greater than 1 mg/ml, approximately, a 30% loss of enzymatic activity occurs during 1 year
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DEAE column chromatography and TEAE cellulose column chromatography, and ammonium sulfate precipitation
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DEAE-cellulose column chromatography, cellulose phosphate column chromatography, ammonium sulfate fractionation, TEAE-cellulose column chromatography, and Sephadex G-200 gel filtration
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His-tag affinity column chromatography
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Profinity IMAC resin column chromatography
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expressed in Escherichia coli BL21(DE3)pLysS cells
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Zhang, B.; Lingga, C.; Bowman, C.; Hackmann, T.J.
A new pathway for forming acetate and synthesizing ATP during fermentation in bacteria
Appl. Environ. Microbiol.
87
e0295920
2021
Cutibacterium granulosum, Cutibacterium granulosum VPI 0507
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Haller, T.; Buckel, T.; Retey, J.; Gerlt, J.
Discovering new enzymes and metabolic pathways Conversion of succinate to propionate by Escherichia coli
Biochemistry
39
4622-4629
2000
Escherichia coli, Escherichia coli 1655
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Schulz, T.K.F.; Kluytmans, J.J.
Pathway of propionate synthesis in the sea mussel Mytilus edulis L.
Comp. Biochem. Physiol. B
75
365-372
1983
Mytilus edulis
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brenda
Allen, S.H.; Kellermeyer, R.W.; Stjernholm, R.L.; Wood, H.G.
Purification and properties of enzymes involved in the propionic acid fermentation
J. Bacteriol.
87
171-187
1964
Propionibacterium freudenreichii subsp. shermanii, Propionibacterium freudenreichii subsp. shermanii 52W
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Schulman, M.; Wood, H.
Succinyl-CoA propionate CoA-transferase from Propionibacterium shermanii EC 2.8.3.6 succinyl-CoA propionate CoA-transferase
Methods Enzymol.
35
235-242
1975
Propionibacterium freudenreichii subsp. shermanii, Propionibacterium freudenreichii subsp. shermanii 52W
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van Grinsven, K.; van Hellemond, J.; Tielens, A.
Acetate succinate CoA-transferase in the anaerobic mitochondria of Fasciola hepatica
Mol. Biochem. Parasitol.
164
74-79
2009
Fasciola hepatica
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