Information on EC 2.8.3.24 - (R)-2-hydroxy-4-methylpentanoate CoA-transferase

for references in articles please use BRENDA:EC2.8.3.24
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The expected taxonomic range for this enzyme is: Clostridioides difficile

EC NUMBER
COMMENTARY hide
2.8.3.24
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RECOMMENDED NAME
GeneOntology No.
(R)-2-hydroxy-4-methylpentanoate CoA-transferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate = 4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-leucine degradation IV (Stickland reaction)
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SYSTEMATIC NAME
IUBMB Comments
4-methylpentanoyl-CoA:(R)-2-hydroxy-4-methylpentanoate CoA-transferase
The enzyme, characterized from the bacterium Peptoclostridium difficile, participates in an L-leucine fermentation pathway. The reaction proceeds via formation of a covalent anhydride intermediate between a conserved aspartate residue and the acyl group of the CoA thioester substrate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
show the reaction diagram
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
4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate
4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroxylamine
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after incubation with 200 mM hydroxylamine at pH 7.0 in the presence of 0.2 mM (R)-2-hydroxyisocaproyl-CoA and removal of the small molecules by gel filtration, the transferase sample shows 94% inactivation, while no inactivation is observed under the same conditions in the absence of (R)-2-hydroxyisocaproyl-CoA
NaBH4
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after incubation with 20 mM NaBH4 at pH 7.0 in the presence of 0.2 mM (R)-2-hydroxyisocaproyl-CoA and removal of the small molecules by gel filtration, the transferase sample shows 88% inactivation, while no inactivation is observed under the same conditions in the absence of (R)-2-hydroxyisocaproyl-CoA
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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2 * 43000, C-terminal Strep tag II fusion protein, SDS-PAGE
86000
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C-terminal Strep tag II fusion protein, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpresssion in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D171A
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the mutant enzyme is more than 2000-fold less active than the wild-type enzyme
D171N
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the mutant enzyme is more than 2000-fold less active than the wild-type enzyme
D171A
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the mutant enzyme is more than 2000-fold less active than the wild-type enzyme
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D171N
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the mutant enzyme is more than 2000-fold less active than the wild-type enzyme
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