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Information on EC 2.8.3.20 - succinyl-CoA-D-citramalate CoA-transferase for references in articles please use BRENDA:EC2.8.3.20
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EC Tree
IUBMB Comments The enzyme, purified from the bacterium Clostridium tetanomorphum, can also accept itaconate as acceptor, with lower efficiency.
The enzyme appears in viruses and cellular organisms
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SCT
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succinyl-CoA + (R)-citramalate = succinate + (R)-citramalyl-CoA
succinyl-CoA + (R)-malate = succinate + (R)-malyl-CoA
succinyl-CoA + (R)-citramalate = succinate + (R)-citramalyl-CoA
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succinyl-CoA + (R)-citramalate = succinate + (R)-citramalyl-CoA
(1)
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succinyl-CoA + (R)-citramalate = succinate + (R)-citramalyl-CoA
(1)
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succinyl-CoA + (R)-citramalate = succinate + (R)-citramalyl-CoA
(1)
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succinyl-CoA + (R)-malate = succinate + (R)-malyl-CoA
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succinyl-CoA + (R)-malate = succinate + (R)-malyl-CoA
(2)
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succinyl-CoA + (R)-malate = succinate + (R)-malyl-CoA
(2)
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succinyl-CoA + (R)-malate = succinate + (R)-malyl-CoA
(2)
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succinyl-CoA:(R)-citramalate CoA-transferase
The enzyme, purified from the bacterium Clostridium tetanomorphum, can also accept itaconate as acceptor, with lower efficiency.
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succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
succinyl-CoA + (R)-malate
succinate + (R)-malyl-CoA
succinyl-CoA + itaconate
succinate + ?
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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-
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?
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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the enzyme catalyzes a steps in the glyoxylate assimilation route
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?
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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?
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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the enzyme catalyzes a steps in the glyoxylate assimilation route
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?
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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?
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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the enzyme catalyzes a steps in the glyoxylate assimilation route
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?
succinyl-CoA + (R)-malate
succinate + (R)-malyl-CoA
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88% compared to the activity with (R)-citramalate
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?
succinyl-CoA + (R)-malate
succinate + (R)-malyl-CoA
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88% compared to the activity with (R)-citramalate
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?
succinyl-CoA + (R)-malate
succinate + (R)-malyl-CoA
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88% compared to the activity with (R)-citramalate
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?
succinyl-CoA + itaconate
succinate + ?
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80% compared to the activity with (R)-citramalate
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?
succinyl-CoA + itaconate
succinate + ?
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80% compared to the activity with (R)-citramalate
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?
succinyl-CoA + itaconate
succinate + ?
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80% compared to the activity with (R)-citramalate
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?
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succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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the enzyme catalyzes a steps in the glyoxylate assimilation route
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?
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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the enzyme catalyzes a steps in the glyoxylate assimilation route
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?
succinyl-CoA + (R)-citramalate
succinate + (R)-citramalyl-CoA
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the enzyme catalyzes a steps in the glyoxylate assimilation route
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?
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additional information
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activity is not dependent on Mg2+
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2.2
(R)-citramalate
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55°C, pH and temperature not specified in the publication
0.08
succinyl-CoA
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55°C, pH and temperature not specified in the publication
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13
(R)-citramalate
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55°C, pH and temperature not specified in the publication
13
succinyl-CoA
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55°C, pH and temperature not specified in the publication
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17.5
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55°C, pH and temperature not specified in the publication
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brenda
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brenda
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physiological function
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the enzyme catalyzes a steps in the glyoxylate assimilation route
physiological function
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the enzyme catalyzes a steps in the glyoxylate assimilation route
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physiological function
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the enzyme catalyzes a steps in the glyoxylate assimilation route
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SCCT_CHLAA
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
402
0
44033
Swiss-Prot
A0A0X8R061_9SPHN
388
0
41237
TrEMBL
A0A383RZA3_9PSED
399
0
43305
TrEMBL
A0A1D3K311_9PSED
399
0
43580
TrEMBL
A0A375H003_9BURK
398
0
42318
TrEMBL
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44000
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2 * 44000, SDS-PAGE
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homodimer
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2 * 44000, SDS-PAGE
homodimer
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2 * 44000, SDS-PAGE
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homodimer
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2 * 44000, SDS-PAGE
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4°C, pH 7, 1 week, in the presence of 100 mM KCl, without significant loss of activity
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frozen for months in the presence of 10% glycerol (v/v), without significant loss of activity
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heterologously expressed in Escherichia coli
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upregulated under autotrophic conditions
upregulated under autotrophic conditions
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upregulated under autotrophic conditions
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upregulated under autotrophic conditions
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Friedmann, S.; Alber, B.E.; Fuchs, G.
Properties of succinyl-coenzyme A:D-citramalate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus
J. Bacteriol.
188
6460-6468
2006
Chloroflexus aurantiacus, Chloroflexus aurantiacus DSM 636
brenda
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2.8.3.20 succinyl-CoA-D-citramalate CoA-transferase
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