Enzymes
UniProtKB help_outline | 2,475 proteins |
Reaction participants Show >> << Hide
- Name help_outline a (3S)-3-hydroxyacyl-CoA Identifier CHEBI:57318 Charge -4 Formula C24H35N7O18P3SR SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)C[C@@H](O)[*] 2D coordinates Mol file for the small molecule Search links Involved in 44 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a (2E)-enoyl-CoA Identifier CHEBI:58856 Charge -4 Formula C24H33N7O17P3SR SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)\C=C\[*] 2D coordinates Mol file for the small molecule Search links Involved in 230 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:16105 | RHEA:16106 | RHEA:16107 | RHEA:16108 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Specific form(s) of this reaction
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Publications
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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-Mueller R., Guehnemann-Schaefer K., Kindl H.
Peroxisomes from different eukaryotic organisms house a multifunctional protein acting in fatty acid beta-oxidation. In plant glyoxysomes, one of the isoforms of this protein contains the activities of L-3-hydroxyacyl-CoA hydrolyase (EC 4.2.1.17), L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211), ... >> More
Peroxisomes from different eukaryotic organisms house a multifunctional protein acting in fatty acid beta-oxidation. In plant glyoxysomes, one of the isoforms of this protein contains the activities of L-3-hydroxyacyl-CoA hydrolyase (EC 4.2.1.17), L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211), D-3-hydroxyacyl-CoA epimerase, and delta 3,delta 2-enoyl-CoA isomerase (EC 5.3.3.8). This was demonstrated after molecular cloning of a cDNA coding for a protein of 79047 Da and its bacterial expression. Chromatographic purification yielded a monomeric protein exhibiting all four activities. In addition, mutant forms were prepared, and peptides representing single domains were purified. Peptides containing the N-terminal region showed D-3-hydroxyacyl-CoA epimerase and delta 3,delta 2-enoyl-CoA isomerase activities but lacked 2-trans-enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenase activities. Using the N-terminal fragment, we demonstrated that the D-3-hydroxyacyl-CoA converting activity is actually an epimerase rather than part of a combined water eliminating and water attaching system. The C-terminal half of the multifunctional protein represents the dehydrogenase domain. << Less
J. Biol. Chem. 269:20475-20481(1994) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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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 N.
<h4>Background</h4>Short-chain enoyl-CoA hydratase-ECHS1-catalyses many metabolic pathways, including mitochondrial short-chain fatty acid β-oxidation and branched-chain amino acid catabolic pathways; however, the metabolic products essential for the diagnosis of ECHS1 deficiency have not yet been ... >> More
<h4>Background</h4>Short-chain enoyl-CoA hydratase-ECHS1-catalyses many metabolic pathways, including mitochondrial short-chain fatty acid β-oxidation and branched-chain amino acid catabolic pathways; however, the metabolic products essential for the diagnosis of ECHS1 deficiency have not yet been determined. The objective of this report is to characterise ECHS1 and a mild form of its deficiency biochemically, and to determine the candidate metabolic product that can be efficiently used for neonatal diagnosis.<h4>Methods</h4>We conducted a detailed clinical, molecular genetics, biochemical and metabolic analysis of sibling patients with ECHS1 deficiency. Moreover, we purified human ECHS1, and determined the substrate specificity of ECHS1 for five substrates via different metabolic pathways.<h4>Results</h4>Human ECHS1 catalyses the hydration of five substrates via different metabolic pathways, with the highest specificity for crotonyl-CoA and the lowest specificity for tiglyl-CoA. The patients had relatively high (∼7%) residual ECHS1 enzyme activity for crotonyl-CoA and methacrylyl-CoA caused by the compound heterozygous mutations (c.176A>G, (p.N59S) and c.413C>T, (p.A138V)) with normal mitochondrial complex I-IV activities. Affected patients excrete large amounts of N-acetyl-S-(2-carboxypropyl)cysteine, a metabolite of methacrylyl-CoA.<h4>Conclusions</h4>Laboratory data and clinical features demonstrated that the patients have a mild form of ECHS1 deficiency harbouring defective valine catabolic and β-oxidation pathways. N-Acetyl-S-(2-carboxypropyl) cysteine level was markedly high in the urine of the patients, and therefore, N-acetyl-S-(2-carboxypropyl)cysteine was regarded as a candidate metabolite for the diagnosis of ECHS1 deficiency. This metabolite is not part of current routine metabolic screening protocols, and its inclusion, therefore, holds immense potential in accurate diagnosis. << Less
J. Med. Genet. 52:691-698(2015) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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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 S.D.X., Mullen R.T., Muench D.G.
The control of subcellular mRNA localization and translation is often mediated by protein factors that are directly or indirectly associated with the cytoskeleton. We report the identification and characterization of a rice seed protein that possesses both RNA and microtubule binding activities. I ... >> More
The control of subcellular mRNA localization and translation is often mediated by protein factors that are directly or indirectly associated with the cytoskeleton. We report the identification and characterization of a rice seed protein that possesses both RNA and microtubule binding activities. In vitro UV cross-linking assays indicated that this protein binds to all mRNA sequences tested, although there was evidence for preferential binding to RNAs that contained A-C nucleotide sequence motifs. The protein was purified to homogeneity using a two-step procedure, and amino acid sequencing identified it as the multifunctional protein (MFP), a peroxisomal enzyme known to possess a number of activities involved in the beta-oxidation of fatty acids. The recombinant version of this rice MFP binds to RNA in UV cross-linking and gel mobility shift experiments, co-sediments specifically with microtubules, and possesses at least two enzymatic activities involved in peroxisomal fatty acid beta-oxidation. Taken together these data suggest that MFP has an important role in mRNA physiology in the cytoplasm, perhaps in regulating the localization or translation of mRNAs through an interaction with microtubules, in addition to its peroxisomal function. << Less
J. Biol. Chem. 277:2419-2429(2002) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis.
Johansson P., Castell A., Jones T.A., Backbro K.
A large fraction of the Mycobacterium tuberculosis genome codes for proteins of unknown function. We here report the structure of one of these proteins, Rv0130, solved to a resolution of 1.8 å. The Rv0130 monomer features a single hotdog fold composed of a highly curved beta-sheet on top of a long ... >> More
A large fraction of the Mycobacterium tuberculosis genome codes for proteins of unknown function. We here report the structure of one of these proteins, Rv0130, solved to a resolution of 1.8 å. The Rv0130 monomer features a single hotdog fold composed of a highly curved beta-sheet on top of a long and a short alpha-helix. Two monomers in turn pack to form a double-hotdog-folded homodimer, similar to a large group of enzymes that use thiol esters as substrates. Rv0130 was found to contain a highly conserved R-specific hydratase motif buried deeply between the two monomers. Our biochemical studies show that the protein is able to hydrate a short trans-2-enoyl-coenzyme A moiety with a k(cat) of 1.1 x 10(2) sec(-1). The importance of the side chains of D40 and H45 for hydratase activity is demonstrated by site-directed mutagenesis. In contrast to many hotdog-folded proteins, a proline residue distorts the central helix of Rv0130. This distortion allows the creation of a long, curved tunnel, similar to the substrate-binding channels of long-chain eukaryotic hydratase 2 enzymes. << Less
Protein Sci. 15:2300-2309(2006) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.