Information on EC 2.8.3.13 - succinate-hydroxymethylglutarate CoA-transferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.8.3.13
-
RECOMMENDED NAME
GeneOntology No.
succinate-hydroxymethylglutarate CoA-transferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + 3-hydroxy-3-methylglutarate = succinate + (S)-3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
malonyl-CoA can also act as donor, but more slowly
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine degradation IV
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-
L-lysine degradation V
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L-lysine degradation X
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SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:3-hydroxy-3-methylglutarate CoA-transferase
Malonyl-CoA can also act as donor, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
80237-90-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxy-3-methylglutaryl-CoA + adipate
3-hydroxy-3-methylglutarate + adipyl-CoA
show the reaction diagram
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + glutarate
3-hydroxy-3-methylglutarate + glutaryl-CoA
show the reaction diagram
3-hydroxy-3-methylglutaryl-CoA + malonate
3-hydroxy-3-methylglutarate + malonyl-CoA
show the reaction diagram
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + methylmalonate
3-hydroxy-3-methylglutarate + methylmalonyl-CoA
show the reaction diagram
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + succinate
3-hydroxy-3-methylglutarate + succinyl-CoA
show the reaction diagram
adipyl-CoA + 3-hydroxy-3-methylglutarate
adipate + 3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
adipyl-CoA + glutarate
adipate + glutaryl-CoA
show the reaction diagram
-
forward reaction at 82%, reverse reaction at 68% the rate of the CoA-transfer between adipyl-CoA and succinate
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r
adipyl-CoA + malonate
adipate + malonyl-CoA
show the reaction diagram
-
forward reaction at 40%, reverse reaction at 43% the rate of the CoA-transfer between adipyl-CoA and succinate
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r
adipyl-CoA + methylmalonate
adipate + methylmalonyl-CoA
show the reaction diagram
-
poor substrate, succinyl-CoA, glutaryl-CoA, malonyl-CoA or 3-hydroxy-3-methylglutaryl-CoA can replace adipyl-CoA
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r
adipyl-CoA + succinate
adipate + succinyl-CoA
show the reaction diagram
-
best substrates, reverse reaction at 38% the rate of forward reaction
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r
butyryl-CoA + 3-hydroxy-3-methylglutarate
butyrate + 3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
-
only negligible amounts of HMGCoA produced
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?
glutaryl-CoA + 3-hydroxy-3-methylglutarate
glutarate + 3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
-
forward and reverse reaction at 50% the rate of the CoA-transfer between adipyl-CoA and succinate
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r
glutaryl-CoA + adipate
glutarate + adipyl-CoA
show the reaction diagram
-
-
-
r
glutaryl-CoA + malonate
glutarate + malonyl-CoA
show the reaction diagram
-
forward reaction at 33%, reverse reaction at 41% the rate of the CoA-transfer between adipyl-CoA and succinate
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r
glutaryl-CoA + methylmalonate
glutarate + methylmalonyl-CoA
show the reaction diagram
-
-
-
r
glutaryl-CoA + succinate
glutarate + succinyl-CoA
show the reaction diagram
-
-
-
r
malonyl-CoA + 3-hydroxy-3-methylglutarate
malonate + 3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
malonyl-CoA + adipate
malonate + adipyl-CoA
show the reaction diagram
-
-
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r
malonyl-CoA + glutarate
malonate + glutaryl-CoA
show the reaction diagram
-
-
-
r
malonyl-CoA + methylmalonate
malonate + methylmalonyl-CoA
show the reaction diagram
-
-
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r
malonyl-CoA + succinate
malonate + succinyl-CoA
show the reaction diagram
-
-
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r
methylmalonyl-CoA + 3-hydroxy-3-methylglutarate
methylmalonate + 3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
-
-
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r
methylmalonyl-CoA + adipate
methylmalonate + adipyl-CoA
show the reaction diagram
-
-
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r
methylmalonyl-CoA + glutarate
methylmalonate + glutaryl-CoA
show the reaction diagram
-
-
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r
methylmalonyl-CoA + malonate
methylmalonate + malonyl-CoA
show the reaction diagram
-
-
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r
methylmalonyl-CoA + succinate
methylmalonate + succinyl-CoA
show the reaction diagram
-
-
-
r
succinyl-CoA + 3-hydroxy-3-methylglutarate
succinate + 3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
succinyl-CoA + adipate
succinate + adipyl-CoA
show the reaction diagram
-
-
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r
succinyl-CoA + glutarate
succinate + glutaryl-CoA
show the reaction diagram
-
forward reaction at 58%, reverse reaction at 55% the rate of the CoA-transfer between adipyl-CoA and succinate
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r
succinyl-CoA + malonate
succinate + malonyl-CoA
show the reaction diagram
-
forward reaction at 29%, reverse reaction at 22% the rate of the CoA-transfer between adipyl-CoA and succinate
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r
succinyl-CoA + methylmalonate
succinate + methylmalonyl-CoA
show the reaction diagram
-
-
-
r
additional information
?
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adipate, 3-hydroxy-3-methylglutarate and itaconate are at least 10% as good as succinate in a reaction where glutaryl-CoA is used as CoA donor. Other, shorter (malonate, methylmalonate) or more polar (D- and L-2-hydroxyglutarate, malate, alpha-ketoglutarate) are poorer substrates, which react at rates between 1 and 10% of that observed with succinate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + 3-hydroxy-3-methylglutarate
succinate + 3-hydroxy-3-methylglutaryl-CoA
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetoacetate
acetoacetyl-CoA
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non-competitive inhibition
acetyl-CoA
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non-competitive inhibition
butyryl-CoA
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non-competitive inhibition
carnitine
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Cl-
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high concentration
ClO4-
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high concentration
coenzyme A
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non-competitive inhibition
F-
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high concentration
I-
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high concentration
malonate
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competitive inhibition
succinate
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competitive inhibition of the product
additional information
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only negligibly affected by sulfhydryl reagents and by the cations Li+, Cd2+, Ca2+, Mg2+, Mn2+ and Fe2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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increases activity
additional information
-
not activated by 2-mercaptoethanol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76 - 2.33
3-hydroxy-3-methylglutarate
0.18 - 0.62
3-hydroxy-3-methylglutaryl-CoA
0.39 - 1.51
adipate
0.07 - 0.4
adipyl-CoA
0.18 - 0.84
Glutarate
0.07 - 0.73
glutaryl-CoA
1.01 - 1.71
malonate
0.13 - 0.7
malonyl-CoA
1.95 - 3.05
methylmalonate
0.65 - 0.87
methylmalonyl-CoA
0.5 - 1.2
succinate
0.15 - 0.83
succinyl-CoA
0.75
succinylCoA
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pH 7.8, 30C, cosubstrate malonate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
acetoacetate
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pH 8.5, 30C
2.1
malonate
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pH 8.5, 30C
1.5
succinate
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pH 8.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
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gel filtration
48000 - 52000
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gel filtration
50000
x * 50000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, SDS-PAGE
tetramer
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4 * 12000-14000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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decreasing the pH to lower values causes an irreversible loss of the enzyme activity
643832
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 3mg/ml bovine serum albumin slightly increases stability, 10% glycerol stabilizes
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mercaptoethanol improves stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.1 M KH2PO4, pH 7.8, retains 70% of its activity after 2 months of storage
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-20C, enzyme preparation with glycerol and mercaptoethanol retains 80% of its activity after 2 week of storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells and HEK-293T cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R336W
inactive