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

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EC Tree

2 Transferases

2.8 Transferring sulfur-containing groups

2.8.3 CoA-transferases

2.8.3.24 (R)-2-hydroxy-4-methylpentanoate CoA-transferase

IUBMB Comments

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.

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The expected taxonomic range for this enzyme is: Clostridioides difficile

Reaction Schemes

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4-methylpentanoyl-CoA

(R)-2-hydroxy-4-methylpentanoate

4-methylpentanoate

(R)-2-hydroxy-4-methylpentanoyl-CoA

Synonyms

(R)-2-hydroxyisocaproate CoA transferase, HadA, show all synonyms

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

(R)-2-hydroxyisocaproate CoA transferase

2 entries

HadA

2 entries

(R)-2-hydroxyisocaproate CoA transferase

Clostridioides difficile

671476

(R)-2-hydroxyisocaproate CoA transferase

Clostridioides difficile DSM 1296T

HadA

Clostridioides difficile

671476

HadA

Clostridioides difficile DSM 1296T

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate = 4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA

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PATHWAY SOURCE

PATHWAYS

BRENDA

leucine metabolism

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SYSTEMATIC NAME

IUBMB Comments

4-methylpentanoyl-CoA:(R)-2-hydroxy-4-methylpentanoate CoA-transferase

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

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

4 entries

4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate

4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA

Clostridioides difficile

the enzyme participates in an L-leucine fermentation pathway

671476

4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate

4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA

Clostridioides difficile

the reaction proceeds via formation of a covalent anhydride intermediate between a conserved aspartate residue and the acyl group of the CoA thioester substrate. Other CoA thioesters, such as acetyl-CoA or butyryl-CoA, are not accepted as substrates. Unexpectedly, CoA transfers from chemically synthesized (E)-2-isocaprenoyl-CoA to (R)-2-hydroxyisocaproate or to isocaproate cand not be observed

671476

4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate

4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA

Clostridioides difficile DSM 1296T

the enzyme participates in an L-leucine fermentation pathway

671476

4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate

4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA

Clostridioides difficile DSM 1296T

671476

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

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

2 entries

4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate

4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA

Clostridioides difficile

the enzyme participates in an L-leucine fermentation pathway

671476

4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate

4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA

Clostridioides difficile DSM 1296T

the enzyme participates in an L-leucine fermentation pathway

671476

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

hydroxylamine

Clostridioides difficile

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

671476

NaBH4

Clostridioides difficile

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

671476

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Clostridioides difficile

671476

brenda

Clostridioides difficile DSM 1296T

671476

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

metabolism

2 entries

metabolism

Clostridioides difficile

the enzyme participates in an L-leucine fermentation pathway

671476

metabolism

Clostridioides difficile DSM 1296T

the enzyme participates in an L-leucine fermentation pathway

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

43000

Clostridioides difficile

2 * 43000, C-terminal Strep tag II fusion protein, SDS-PAGE

671476

86000

Clostridioides difficile

C-terminal Strep tag II fusion protein, gel filtration

671476

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

homodimer

2 entries

homodimer

Clostridioides difficile

2 * 43000, C-terminal Strep tag II fusion protein, SDS-PAGE

671476

homodimer

Clostridioides difficile DSM 1296T

2 * 43000, C-terminal Strep tag II fusion protein, SDS-PAGE

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D171A

Clostridioides difficile

the mutant enzyme is more than 2000-fold less active than the wild-type enzyme

671476

D171N

Clostridioides difficile

the mutant enzyme is more than 2000-fold less active than the wild-type enzyme

671476

D171A

Clostridioides difficile DSM 1296T

the mutant enzyme is more than 2000-fold less active than the wild-type enzyme

D171N

Clostridioides difficile DSM 1296T

the mutant enzyme is more than 2000-fold less active than the wild-type enzyme

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

Clostridioides difficile

671476

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

overexpresssion in Escherichia coli

Clostridioides difficile

671476

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

671476

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.

6062-6069

2006

Clostridioides difficile, Clostridioides difficile DSM 1296T

16957230

brenda

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