| enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase | |||||||
|---|---|---|---|---|---|---|---|
 The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa [1] | |||||||
| Identifiers | |||||||
| Symbol | EHHADH | ||||||
| Alt. symbols | ECHD | ||||||
| NCBI gene | 1962 | ||||||
| HGNC | 3247 | ||||||
| OMIM | 607037 | ||||||
| RefSeq | NM_001966 | ||||||
| UniProt | Q08426 | ||||||
| Other data | |||||||
| EC number | 4.2.1.17 | ||||||
| Locus | Chr. 3 q26.3-q28 | ||||||
| |||||||
3-Hydroxyacyl ACP dehydrase is an enzyme involved in fatty acid synthesis.
In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible. For example, an enzyme that catalyzed this reaction would be a lyase:
Dehydratases are a group of lyase enzymes that form double and triple bonds in a substrate through the removal of water. They can be found in many places including the mitochondria, peroxisome and cytosol. There are more than 150 different dehydratase enzymes that are classified into four groups. Dehydratases can act on hydroxyacyl-CoA with or without cofactors, and some have a metal and non-metal cluster act as their active site.
Polyketide synthases (PKSs) are a family of multi-domain enzymes or enzyme complexes that produce polyketides, a large class of secondary metabolites, in bacteria, fungi, plants, and a few animal lineages. The biosyntheses of polyketides share striking similarities with fatty acid biosynthesis.
Trifunctional enzyme subunit alpha, mitochondrial also known as hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase, alpha subunit is a protein that in humans is encoded by the HADHA gene. Mutations in HADHA have been associated with trifunctional protein deficiency or long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency.
Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structural and chemical properties vary greatly among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. The reaction it catalyzes is the deamination of L-serine to yield pyruvate, with the release of ammonia.
In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction
Delta-aminolevulinic acid dehydratase (porphobilinogen synthase, or ALA dehydratase, or aminolevulinate dehydratase) is an enzyme (EC 4.2.1.24) that in humans is encoded by the ALAD gene. Porphobilinogen synthase (or ALA dehydratase, or aminolevulinate dehydratase) synthesizes porphobilinogen through the asymmetric condensation of two molecules of aminolevulinic acid. All natural tetrapyrroles, including hemes, chlorophylls and vitamin B12, share porphobilinogen as a common precursor. Porphobilinogen synthase is the prototype morpheein.
In enzymology, a 2-methylcitrate dehydratase (EC 4.2.1.79) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.61) is an enzyme that catalyzes the chemical reaction
PHS1 may refer to:
Fatty-acyl-CoA Synthase, or more commonly known as yeast fatty acid synthase, is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.
D-bifunctional protein (DBP), also known as peroxisomal multifunctional enzyme type 2 (MFP-2), as well as 17β-hydroxysteroid dehydrogenase type IV is a protein that in humans is encoded by the HSD17B4 gene. It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and steroid metabolism.
3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase (EC 4.2.1.60, D-3-hydroxydecanoyl-[acyl-carrier protein] dehydratase, 3-hydroxydecanoyl-acyl carrier protein dehydrase, 3-hydroxydecanoyl-acyl carrier protein dehydratase, beta-hydroxydecanoyl thioester dehydrase, beta-hydroxydecanoate dehydrase, beta-hydroxydecanoyl thiol ester dehydrase, FabA, beta-hydroxyacyl-acyl carrier protein dehydratase, HDDase, beta-hydroxyacyl-ACP dehydrase, (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] hydro-lyase) is an enzyme with systematic name (3R)-3-hydroxydecanoyl-(acyl-carrier protein) hydro-lyase. This enzyme catalyses the following chemical reaction
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase is an enzyme with systematic name very-long-chain (3R)-3-hydroxyacyl-CoA hydro-lyase. This enzyme catalyses the following chemical reaction
Elongase is a generic term for an enzyme that catalyzes carbon chain extension of an organic molecule, especially a fatty acid. Elongases play a variety of roles in mammalian organisms, accounting for changes in tissue function, lipid regulation, and the overall physiology of an organism.
Hydroxyacyl-thioester dehydratase type 2 is a protein that in humans is encoded by the HTD2 gene.
3-hydroxyacyl-CoA dehydratase 2 is a protein that in humans is encoded by the HACD2 gene.
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