Hydratase

2-Enoyl-Coenzyme A (CoA) Hydratase, Beta (HADHB) is the beta subunit of the mitochondrial trifunctional protein, that catalyzes the last 3 phases of mitochondrial beta-oxidation of long chain fatty acids. HADHB binds RNA and reduces the stability of various mRNAs. Mutations in HADHB cause trifunctional protein deficiency.

GMDS is a member of the GDP-mannose 4,6-dehydratase family. GMDS uses NADP as a cofactor to catalyze the conversion of GDP-mannose to GDP-4-keto-6-deoxymannose. Defects in the gene encoding GMDS cause TRAIL (tumor necrosis factor-related apoptosis-inducing ligand)-induced apoptosis.

Fumarase is an enzymatic factor of Krebs cycle, which catalyzes the formation of L-malate from fumarate. Fumarase exists in both a cytosolic form and an N-terminal extended form, differing only in the translation start site used. The N-terminal extended form is aimed to the mitochondrion, where the removal of the extension results in the same form as in the cytoplasm. Fumarase is similar to a number of thermostable Class-2 fumarases and functions as a homotetramer. Mutations in the Fumarase gene causes fumarase deficiency and leads to progressive encephalopathy, cerebral atrophy and developmental delay. Fumarase enzyme is also thought to act as a tumor suppressor. Leydig cell tumors are caused by Fumarase mutations and represents one of the first reports of germline mutations in any type of adult testicular tumor.

PCBD1 enzyme takes part in phenylalanine hydroxylation. PCBD1 deficiency results in hyperphenylalaninemia. PCBD1 enzyme controls the homodimerization of HNF1. PCBD1 takes part in tetrahydrobiopterin biosynthesis. PCBD1 prevents the formation of 7-pterins and accelerate the formation of quinonoid-BH2. PCBD1 is a coactivator for HNF1A-dependent transcription.

Mitochondrial methylglutaconyl-CoA hydratase (AUH) is involved in the amino acid degradation pathway by catalyzing the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA and water. AUH Human is expressed as a single mRNA species of 1.8 kb, and translated as a 40kDa precursor protein which is consequently processed to a 32kDa mature form. AUH has a very low enoyl-CoA hydratase activity. The AUH protein binds to the AU-rich element (ARE), which is a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. AU-rich elements are involved in directing RNA to rapid degradation and deadenylation. In addition, AUH is homologous to enol-CoA hydratase, which is an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is therefore a bifunctional chimera between RNA binding and metabolic enzyme activity.

ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

Enoyl CoA hydratase domain containing 1 (ECHDC1) is a member of the enoyl-CoA hydratase/isomerase family. ECHDC1 is an enzyme which hydrates the double bond between the second and third carbons on acyl-CoA. The ECHDC1 enzyme is crucial to metabolizing fatty acids to supply both acetyl CoA and energy.

ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.

ALAD form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins) by catalyzing the compression of 2 molecules of delta-aminolevulinate. ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is vital for enzymatic activity. ALAD has 8 identical subunits and its enzymatic activity is inhibited by lead. Mutations in the ALAD structural gene are the source for high sensitivity to lead poisoning and acute hepatic porphyria.