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Synonyms
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isocaprenoyl-CoA:2-hydroxyisocaproate CoA-transferase
HadA
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isocaprenoyl-CoA:2-hydroxyisocaproate CoA-transferase
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isocaprenoyl-CoA:2-hydroxyisocaproate CoA-transferase
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4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate = 4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
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4-methylpent-2-enoyl-CoA:(R)-2-hydroxy-4-methylpentanoate CoA-transferase
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4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Substrates: the enzyme is involved in the reductive branch of L-leucine fermentation
?
4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Substrates: i.e. isocaprenoyl-CoA. Acetyl-CoA or butyryl-CoA, are not accepted as substrates. The enzymatically in situ-produced 2-isocaprenoyl-CoA is accepted as a substrate of the CoA transferase and mediates the tranfer to (R)-2-hydroxy-4-methylpentanoate. CoA transfers from chemically synthesized (E)-2-isocaprenoyl-CoA to (R)-2-hydroxyisocaproate or to isocaproate can not be observed
r
4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Substrates: the enzyme is involved in the reductive branch of L-leucine fermentation
?
4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Substrates: i.e. isocaprenoyl-CoA. Acetyl-CoA or butyryl-CoA, are not accepted as substrates. The enzymatically in situ-produced 2-isocaprenoyl-CoA is accepted as a substrate of the CoA transferase and mediates the tranfer to (R)-2-hydroxy-4-methylpentanoate. CoA transfers from chemically synthesized (E)-2-isocaprenoyl-CoA to (R)-2-hydroxyisocaproate or to isocaproate can not be observed
r
4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Substrates: i.e. isocaproyl-CoA. Acetyl-CoA or butyryl-CoA, are not accepted as substrates. CoA transfers from chemically synthesized (E)-2-isocaprenoyl-CoA to (R)-2-hydroxyisocaproate or to isocaproate can not be observed
r
4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Substrates: i.e. isocaproyl-CoA. Acetyl-CoA or butyryl-CoA, are not accepted as substrates. CoA transfers from chemically synthesized (E)-2-isocaprenoyl-CoA to (R)-2-hydroxyisocaproate or to isocaproate can not be observed
r
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4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Substrates: the enzyme is involved in the reductive branch of L-leucine fermentation
?
4-methylpent-2-enoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpent-2-enoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Substrates: the enzyme is involved in the reductive branch of L-leucine fermentation
?
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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metabolism
the enzyme is involved in the reductive branch of L-leucine fermentation
metabolism
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the enzyme is involved in the reductive branch of L-leucine fermentation
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Q5U921_CLODI
398
0
44103
TrEMBL
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43000
2 * 43000, SDS-PAGE
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homodimer
2 * 43000, SDS-PAGE
homodimer
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2 * 43000, SDS-PAGE
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D171A
mutant enzyme is more than 2000fold less active than the wild-type enzyme
D171N
mutant enzyme is more than 2000fold less active than the wild-type enzyme
D171A
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mutant enzyme is more than 2000fold less active than the wild-type enzyme
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D171N
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mutant enzyme is more than 2000fold less active than the wild-type enzyme
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expression in Escherichia coli as N- and C-terminal Strep tag II fusion protein
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Kim, J.; Darley, D.; Selmer, T.; Buckel, W.
Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile
Appl. Environ. Microbiol.
72
6062-6069
2006
Clostridioides difficile (Q5U921), Clostridioides difficile DSM 1296T (Q5U921)
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