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acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-1-CoA
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
acetyl-CoA + acrylate
acrylyl-CoA + acetate
-
poor substrate
-
-
?
acetyl-CoA + crotonate
crotonyl-CoA + acetate
-
poor substrate
-
-
?
acetyl-CoA + isocrotonate
isocrotonyl-CoA + acetate
-
poor substrate
-
-
?
glutaconyl-CoA + (R)-2-hydroxyglutarate
glutaconate + (R)-2-hydroxyglutaryl-CoA
glutaconyl-CoA + (S)-2-hydroxyglutarate
glutaconate + (S)-2-hydroxyglutaryl-CoA
-
at 60% of the rate with (R)-isomer or glutarate
-
-
?
glutaconyl-CoA + 3-hydroxyglutarate
glutaconate + 3-hydroxyglutaryl-CoA
-
at 20% of the rate with glutarate
-
-
?
glutaconyl-CoA + adipate
glutaconate + adipyl-CoA
-
at 60% of the rate with glutarate
-
-
?
glutaconyl-CoA + butyrate
butyryl-CoA + glutaconate
-
-
-
-
?
glutaconyl-CoA + glutarate
glutaconate + glutaryl-CoA
-
very good substrate
-
?
glutaconyl-CoA + propionate
propanoyl-CoA + glutaconate
-
moderate substrate
-
-
?
glutaryl-CoA + acetate
glutarate + acetyl-CoA
additional information
?
-
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
-
-
?
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
-
-
?
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
-
-
r
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
-
-
?
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
-
only 1-isomer is formed
?
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
very good substrate, broad substrate specificity
-
?, r
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
removal of 3'-phospho group from acetyl-CoA leads to reduced activity
-
?, r
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
involved in glutamate fermentation via hydroxyglutarate pathway, activates glutaconate to glutaconyl-CoA prior to glutaconate decarboxylation
-
?
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
-
-
-
?
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
-
-
-
?
acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
-
-
-
?
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-1-CoA
-
-
-
?
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-1-CoA
-
-
-
r
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-1-CoA
-
-
-
r
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-1-CoA
-
-
?
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-1-CoA
-
-
in vitro formation of both isomers: (R)-2-hydroxyglutaryl-1-CoA and (R)-2-hydroxyglutaryl-5-CoA, the 1-isomer is kinetically favoured, the 5-isomer is thermodynamically favoured
?
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-1-CoA
-
-
in vitro formation of both isomers: (R)-2-hydroxyglutaryl-1-CoA and (R)-2-hydroxyglutaryl-5-CoA, the 1-isomer is kinetically favoured, the 5-isomer is thermodynamically favoured, product in vivo, 5-isomer only occurs in vitro, (R)-2-hydroxyglutaryl-1-CoA is an excellent substrate in the reverse reaction
r
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
-
in the course of glutamate fermentation
-
?
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
-
in the course of glutamate fermentation
-
r
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
-
in the course of glutamate fermentation
-
r
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
involved in the conversion of (R)-2-hydroxyglutarate to crotonyl-CoA in the pathway of glutamate fermentation
-
?
glutaconyl-CoA + (R)-2-hydroxyglutarate
glutaconate + (R)-2-hydroxyglutaryl-CoA
-
-
formation of the 5-isomer, not of the 1-isomer
?
glutaconyl-CoA + (R)-2-hydroxyglutarate
glutaconate + (R)-2-hydroxyglutaryl-CoA
-
very good substrate
generation of both isomers: (R)-2-hydroxyglutaryl-1-CoA and (R)-2-hydroxyglutaryl-5-CoA
?
glutaryl-CoA + acetate
glutarate + acetyl-CoA
-
-
-
?
glutaryl-CoA + acetate
glutarate + acetyl-CoA
-
-
-
r
glutaryl-CoA + acetate
glutarate + acetyl-CoA
-
-
?
glutaryl-CoA + acetate
glutarate + acetyl-CoA
-
exchange of oxygen atoms between the substrates and the catalytic residue betaE-54, exchange is site-specific, reversible and requires both substrates, catalytic mechanism
-
r
additional information
?
-
-
no substrate: lactone-CoA
-
-
?
additional information
?
-
-
wild-type enzyme has significant hydrolase activity using acetyl-CoA as substrate, but no hydrolysis of glutaryl-CoA
-
-
?
additional information
?
-
-
residue E-54 of the subunit GctB is directly involved in catalysis by formation of a CoASH ester intermediate
-
-
?
additional information
?
-
residue E-54 of the small subunit GctB is directly involved in catalysis
-
-
?
additional information
?
-
-
residue E-54 of the small subunit GctB is directly involved in catalysis
-
-
?
additional information
?
-
-
no substrates: (Z)-glutaconate, acetyl-4'-phosphopantetheine, C4-dicarboxylic acids, reverse reaction not with glutamate, 2-oxoglutarate, succinate, malate or citrate
-
-
?
additional information
?
-
-
GCT structure, the active site is located at the interface of subunits A and B and is formed by loops of both subunits
-
-
?
additional information
?
-
-
catalytic residue is E-54 of subunit B, catalytic mechanism
-
-
?
additional information
?
-
-
catalytic residue is E-54 of subunit B, catalytic mechanism
-
-
?
additional information
?
-
-
catalytic residue is E-54 of subunit B, catalytic mechanism
-
-
?
additional information
?
-
-
not involved in the dehydration of (R)-2-hydroxyglutarate to glutaconate
-
-
?
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acetyl-CoA + (E)-glutaconate
acetate + glutaconyl-1-CoA
-
involved in glutamate fermentation via hydroxyglutarate pathway, activates glutaconate to glutaconyl-CoA prior to glutaconate decarboxylation
-
?
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
additional information
?
-
-
not involved in the dehydration of (R)-2-hydroxyglutarate to glutaconate
-
-
?
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
-
in the course of glutamate fermentation
-
?
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
-
in the course of glutamate fermentation
-
r
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
-
in the course of glutamate fermentation
-
r
acetyl-CoA + (R)-2-hydroxyglutarate
acetate + (R)-2-hydroxyglutaryl-CoA
involved in the conversion of (R)-2-hydroxyglutarate to crotonyl-CoA in the pathway of glutamate fermentation
-
?
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260000
-
heterooctamer GCT
29018
-
alpha4beta4, 4 * 35573 + 4 * 29018, MALDI-TOF mass spectrometry
29168
alpha4beta4, 4 * 35725 + 4 * 29168, GctA and GctB, calculated from the DNA sequences
32000
-
alpha4beta4, 4 * 32000 + 4 * 34000, SDS-PAGE
34000
-
alpha4beta4, 4 * 32000 + 4 * 34000, SDS-PAGE
35000
-
alpha4beta4, 4 * 35000 + 4 * 29000, structure and association of the subunits A and B
35573
-
alpha4beta4, 4 * 35573 + 4 * 29018, MALDI-TOF mass spectrometry
35725
alpha4beta4, 4 * 35725 + 4 * 29168, GctA and GctB, calculated from the DNA sequences
29000
-
alpha4beta4, 4 * 36000 + 4 * 29000, GctA and GctB, SDS-PAGE
29000
alpha4beta4, 4 * 36000 + 4 * 29000, GctA and GctB, SDS-PAGE
29000
-
alpha4beta4, 4 * 35000 + 4 * 29000, structure and association of the subunits A and B
36000
-
alpha4beta4, 4 * 36000 + 4 * 29000, GctA and GctB, SDS-PAGE
36000
alpha4beta4, 4 * 36000 + 4 * 29000, GctA and GctB, SDS-PAGE
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E64A
-
mutation in the subunit GctB, 30% as active as wild-type enzyme
E54A
-
mutation in the subunit GctB, inactive mutant
E54A
-
mutant without CoA-transferase or acyl-CoA hydrolase activity
E54A
-
0.02% as active as wild-type enzyme
E54D
-
mutation in the subunit GctB
E54D
-
replacement of the catalytic glutamate by aspartate converts the mutant enzyme to a thiol ester hydrolase
E54D
-
mutation decreases CoA-transferase and increases acyl-CoA hydrolase activity, mechanism, mutant catalyses the hydrolysis of glutaryl-CoA, acetyl-CoA and 3-butenoyl-CoA, mutant Escherichia coli strain shows reduced growth rate after induction
E54D
-
above 7% as active as wild-type enzyme, mutant with changed catalytic mechanism without CoASH intermediate, the Escherichia coli strain producing mutant enzyme shows a lower growth rate and reduced amount of recombinant enzyme
E54N
-
mutation in the subunit GctB, inactive mutant
E54N
-
mutant without CoA-transferase or acyl-CoA hydrolase activity
E54Q
-
mutation in the subunit GctB
E54Q
-
1% as active as wild-type enzyme, by incubating with both substrates for 20 h at room temperature, glutamine is completely converted to glutamate yielding a fully active CoA-transferase
E54Q
-
mutant activity increases from 1% to almost 100% upon incubation with acetyl-CoA and glutaconate at 37°C within 40 h, the substrates induce the conversion of the mutant glutamine residue into the glutamate residue of the wild-type enzyme
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Mack, M.; Buckel, W
Conversion of glutaconate CoA-transferase from Acidaminococcus fermentans into an acyl-CoA hydrolase by site-directed mutagenesis
FEBS Lett.
405
209-212
1997
Acidaminococcus fermentans
brenda
Buckel, W.; Dorn, U.; Semmler, R.
Glutaconate CoA-transferase from Acidaminococcus fermentans
Eur. J. Biochem.
118
315-321
1981
Acidaminococcus fermentans, [Clostridium] symbiosum, [Clostridium] sporosphaeroides, no activity in Clostridium tetanomorphum, [Clostridium] symbiosum HB 25, no activity in Clostridium tetanomorphum H1
brenda
Klees, A.G.; Buckel, W.
Synthesis and properties of (R)-2-hydroxyglutaryl-1-CoA. (R)-2-hydroxyglutaryl-5-CoA, an erroneous product of glutaconate CoA-transferase
Biol. Chem. Hoppe-Seyler
372
319-324
1991
Acidaminococcus fermentans
brenda
Mack, M.; Bendrat, K.; Zelder, O.; Eckel, E.; Linder, D.; Buckel, W.
Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans
Eur. J. Biochem.
226
41-51
1994
Acidaminococcus fermentans (Q59111 and Q59112), Acidaminococcus fermentans
brenda
Mack, M.; Buckel, W.
Identification of glutamate beta54 as the covalent-catalytic residue in the active site of glutaconate CoA-transferase from Acidaminococcus fermentans
FEBS Lett.
357
145-148
1995
Acidaminococcus fermentans
brenda
Jacob, U.; Mack, M.; Clausen, T.; Huber, R.; Buckel, W.; Messerschmidt, A.
Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases
Structure
5
415-426
1997
Acidaminococcus fermentans
brenda
Selmer, T.; Buckel, W.
Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis
J. Biol. Chem.
274
20772-20778
1999
Acidaminococcus fermentans
brenda