Dopamine β-Hydroxylase (DBH) is an enzyme of the copper type II ascorbate-dependent mono-oxygenase family. This enzyme forms homotetramers composed of two noncovalently bound disulfide-linked dimers and is found as both membrane-associated and soluble forms. The soluble form is present in the lumen of secretory granules and is released from cells by exocytosis. DBH converts dopamine to noradrenaline. Deficiency in this enzyme causes a rare disease characterized by a complete absence of noradrenaline and adrenaline in plasma together with increased plasma dopamine levels. Orthostatic hypotension, the main symptom of DBH deficiency, can be alleviated by administration of dihydroxyphenylserine, a synthetic precursor of noradrenaline.
This gene encodes a member of the doublecortin family. The protein encoded by this gene is a cytoplasmic protein and contains two doublecortin domains, which bind microtubules. In the developing cortex, cortical neurons must migrate over long distances to reach the site of their final differentiation. The encoded protein appears to direct neuronal migration by regulating the organization and stability of microtubules. In addition, the encoded protein interacts with LIS1, the regulatory gamma subunit of platelet activating factor acetylhydrolase, and this interaction is important to proper microtubule function in the developing cortex. Mutations in this gene cause abnormal migration of neurons during development and disrupt the layering of the cortex, leading to epilepsy, mental retardation, subcortical band heterotopia ("double cortex" syndrome) in females and lissencephaly.
This gene encodes a member of the doublecortin family. The protein encoded by this gene is a cytoplasmic protein and contains two doublecortin domains, which bind microtubules. In the developing cortex, cortical neurons must migrate over long distances to reach the site of their final differentiation. The encoded protein appears to direct neuronal migration by regulating the organization and stability of microtubules. In addition, the encoded protein interacts with LIS1, the regulatory gamma subunit of platelet activating factor acetylhydrolase, and this interaction is important to proper microtubule function in the developing cortex. Mutations in this gene cause abnormal migration of neurons during development and disrupt the layering of the cortex, leading to epilepsy, cognitive disability, subcortical band heterotopia ("double cortex" syndrome) in females and lissencephaly ("smooth brain" syndrome) in males. Multiple transcript variants encoding different isoforms have been found for this gene.
Hydrolyzes a wide range of dipeptides including the conversion of leukotriene D4 to leukotriene E4. Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation. Possesses also beta lactamase activity and hydrolytically inactivates beta-lactam antibiotics. Independently of its dipeptidase activity acts as an adhesion receptor for neutrophils recruitement from bloodstream into inflammed lungs and liver.
Dipeptidase 3 (DPEP3) is one of three glycosylphosphatidylinositol-anchored metallopeptidases potentially involved in the hydrolytic metabolism of dipeptides. While its exact biological function is not clear, DPEP3 expression is normally limited to testis, but can be elevated in ovarian cancer.
This gene encodes a membrane-bound glycoprotein from the family of dipeptidases involved in hydrolytic metabolism of various dipeptides, including penem and carbapenem beta-lactam antibiotics. This gene is located on chromosome 16 in a cluster with another member of this family. Alternatively spliced transcript variants that encode different isoforms have been found for this gene.
DPP4/CD26 is a type II transmembrane glycoprotein expressed ubiquitously in most tissues and different cell types. The protein has a short cytoplasmic domain, transmembrane domain, a flexible stalk fragment and extracellular fragment. Both the catalytic peptide hydrolase domain and the beta-propeller ligand binding domain are located in the extracellular fragment. DPP4/CD26 is a multifunctional protein that exists in both a membrane bound form as well as an extracellular soluble form. As a peptidase, it removes N-terminal dipeptides sequentially from proteins with a proline or alanine as the penultimate P1 amino acid. DPP4/CD26 has been shown to cleave a wide range of substrates including GLP-1, BNP, etc. In addition to its peptidase activity, DPP4/CD26 interacts with multiple important cell surface ligands, such as adenosine deaminase, fibronectin, and IGF2 receptor to influence processes like T cell activation, cell migration and proliferation.
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