Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.17
Description:Enoyl-CoA hydratase.
Alternative Name: Unsaturated acyl-CoA hydratase.
Enoyl hydrase.
Prosite: PDOC00150;
PDB:
PDBScop
Cath: 1.10.1040.10; 1.10.1040.50; 1.10.12.10; 1.10.287.2460; 1.10.287.3850; 1.20.5.30; 1.20.5.3020; 3.30.160.260; 3.30.300.220; 3.40.50.720;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.17
BRENDA Enzyme Link: BRENDA 4.2.1.17
KEGG Enzyme Link: KEGG4.2.1.17
BioCyc Enzyme Link: BioCyc 4.2.1.17
ExPASy Enzyme Link: ExPASy4.2.1.17
EC2PDB Enzyme Link: EC2PDB 4.2.1.17
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.17
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.17
IntEnz Enzyme Link: IntEnz 4.2.1.17
MEDLINE Enzyme Link: MEDLINE 4.2.1.17
MSA:

4.2.1.17;

Phylogenetic Tree:

4.2.1.17;

Uniprot:
M-CSA:
RHEA:34863 2,3-didehydroadipyl-CoA + H2O = 3-hydroxyadipyl-CoA
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH;+0:2]=[CH;+0:4]-[*:5].[OH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Bacterial phenylalanine and phenylacetate catabolic pathway revealed.Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, Eisenreich W, Haehnel W, Fuchs G2010 Aug 1020660314

RHEA:20724 a 4-saturated-(3S)-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH;+0:3](-[*:4])-[OH;+0:5]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity.Preisig-Müller R, Gühnemann-Schäfer K, Kindl H1994 Aug 128051146
Clinical, biochemical and metabolic characterisation of a mild form of human short-chain enoyl-CoA hydratase deficiency: significance of increased N-acetyl-S-(2-carboxypropyl)cysteine excretion.Yamada K, Aiba K, Kitaura Y, Kondo Y, Nomura N, Nakamura Y, Fukushi D, Murayama K, Shimomura Y, Pitt J, Yamaguchi S, Yokochi K, Wakamatsu N2015 Oct26251176
Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis.Johansson P, Castell A, Jones TA, Bäckbro K2006 Oct16963641
Identification of a rice RNA- and microtubule-binding protein as the multifunctional protein, a peroxisomal enzyme involved in the beta -oxidation of fatty acids.Chuong SD, Mullen RT, Muench DG2002 Jan 2511706039

RHEA:16105 a (3S)-hydroxyacyl-CoA = a (2E)-enoyl CoA + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH;+0:2]=[CH;+0:4]-[*:5].[OH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity.Preisig-Müller R, Gühnemann-Schäfer K, Kindl H1994 Aug 128051146
Clinical, biochemical and metabolic characterisation of a mild form of human short-chain enoyl-CoA hydratase deficiency: significance of increased N-acetyl-S-(2-carboxypropyl)cysteine excretion.Yamada K, Aiba K, Kitaura Y, Kondo Y, Nomura N, Nakamura Y, Fukushi D, Murayama K, Shimomura Y, Pitt J, Yamaguchi S, Yokochi K, Wakamatsu N2015 Oct26251176
Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis.Johansson P, Castell A, Jones TA, Bäckbro K2006 Oct16963641
Identification of a rice RNA- and microtubule-binding protein as the multifunctional protein, a peroxisomal enzyme involved in the beta -oxidation of fatty acids.Chuong SD, Mullen RT, Muench DG2002 Jan 2511706039