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4.2.1.17: enoyl-CoA hydratase

This is an abbreviated version!
For detailed information about enoyl-CoA hydratase, go to the full flat file.

Word Map on EC 4.2.1.17

Reaction

(3S)-3-hydroxyacyl-CoA
=
trans-2(or 3)-enoyl-CoA
 +
H2O

Synonyms

(R)-specific 2-enoyl-CoA hydratase, 2,3-dehydroadipyl-CoA hydratase, 2-enoyl-CoA hydratase, 2-enoyl-CoA hydratase 1, 2-enoyl-CoA hydratase-1, 2-enoyl-hydratase 1, 2-octenoyl coenzyme A hydrase, acyl coenzyme A hydrase, AIM1, AMECH, beta-hydroxyacid dehydrase, beta-hydroxyacyl-CoA dehydrase, CCH/HBCD, classic 2-enoyl-CoA hydratase, crotonase, crotonyl hydrase, crotonyl-CoA hydratase, D-3-hydroxyacyl-CoA dehydratase, DELTA2-enoyl-CoA hydratase-1, ECH, ECH-1, ECH-2, ECH1, ECH2, ECHS1, enol-CoA hydratase, Enoyl coenzyme A hydrase (D), enoyl coenzyme A hydrase (L), enoyl coenzyme A hydratase, enoyl coenzyme A hydratase (L), enoyl coenzyme A hydratase 1, enoyl hydrase, enoyl-CoA hydratase, enoyl-CoA hydratase 1, enoyl-CoA hydratase 2, enoyl-CoA hydratase short chain 1, enoyl-CoA hydratase/isomerase, enoyl-coenzyme A hydratase, enoyl-coenzyme A hydratase/isomerase, FadB', FadRBs, H16_A0461, hydratase, enoyl coenzyme A, mECH-1, MFP2, mitochondrial enoyl coenzyme A hydratase, mitochondrial short-chain enoyl-CoA hydratase, mitochondrial short-chain enoyl-CoA hydratase-1, More, multifunctional enzyme type 1, PaaF, PBE, PBFE, perMFE-1, perMFE-I, peroxisomal bifunctional enzyme, peroxisomal multifunctional enzyme, type 1, R-3-hydroxyacyl-CoA enoyl-CoA hydratase, R-3-hydroxyacyl-CoA enoyl-CoA hydratases, rat peroxisomal multifunctional enzyme type 1, rpMFE1, S-3-hydroxyacyl-CoA enoyl-CoA hydratase, S-3-hydroxyacyl-CoA enoyl-CoA hydratases, SCEH, short chain enoyl coenzyme A hydratase, short-chain enoyl-CoA hydratase, trans-2-enoyl-CoA hydratase, unsaturated acyl-CoA hydratase, YsiA

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.17 enoyl-CoA hydratase

Engineering

Engineering on EC 4.2.1.17 - enoyl-CoA hydratase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A3D/F279S
naturally occuring mutations, identification of heterozygous ECHS1 mutations c.836T>C (novel) (p.F279S) and and c.8C>A (p.A3D) identified by whole exome sequencing, lethal neonatal case. SCEH deficiency is confirmed with very low SCEH activity in fibroblasts and nearly absent immunoreactivity of SCEH. The patient has a severe neonatal course with elevated blood and cerebrospinal fluid (CSF) lactate and pyruvate concentrations, high plasma alanine and slightly low plasma cystine. 2-Methyl-2,3-dihydroxybutyric acid is markedly elevated as are metabolites of the three branched-chain ketoacids on urine organic acids analysis. These urine metabolites notably decrease when lactic acidosis decreases in blood. Lymphocyte pyruvate dehydrogenase complex (PDC) activity is deficient, but PDC and 2-oxoglutarate dehydrogenase complex activities in cultured fibroblasts are normal. Oxidative phosphorylation analysis on intact digitonin-permeabilized fibroblasts is suggestive of slightly reduced PDC activity relative to control range in mitochondria
L230F
naturally occuring mutation
A98P
-
kcat is decreased 3400fold compared to wild type and KM is increased 13fold, mutant enzyme has a severely compromised ability for catalyzing the formation of (3R)-3-hydroxybutanoyl-CoA
E144A
E144A/Q162L
-
kcat for trans-2-hexenoyl-CoA is 12417fold lower than wild-type value. The point mutations E144A and Q162L by themselves apparently do not cause structural rearrangements of the active site helix, but when both residues are changed, the active site geometry changes
E144D
-
60fold decreases in kcat with little change in KM
E144Q
-
3000fold decreases in kcat with little change in KM. The mutant is unable to catalyze the formation of (3R)-3-hydroxybutanoyl-CoA even when the incubation is extended to 4 days
E164A
E164D
-
1200fold decreases in kcat with little change in KM. First-order rate constant for the formation of (3R)-3-hydroxybutanoyl-CoA is similar to wild-type value
E164Q
-
340000fold decreases in kcat with little change in KM. While wild-type enoyl-CoA hydratase catalyzes the rapid interconversion of substrate and the (3S)-3-hydroxybutanoyl-CoA product relative to the rate of (3R)-3-hydroxybutanoyl-CoA formation, E164Q catalyzes the formation of both product enantiomers at similar rates
G141P
-
1600000fold decrease in kcat with no change in KM, mutant enzyme has a severely compromised ability for catalyzing the formation of (3R)-3-hydroxybutanoyl-CoA
Q162A
-
kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
Q162L
-
kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
Q162M
-
kcat for trans-2-hexenoyl-CoA is nearly identical to wild-type value
additional information