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TRHDE
Thyrotropin releasing hormone degrading enzyme is a protein, specifically a pyroglutamyl-peptidase II Pyroglutamyl-peptidase II (, ''thyroliberinase'', ''pyroglutamyl aminopeptidase II'', ''thyrotropin-releasing factor pyroglutamate aminopeptidase'', ''pyroglutamate aminopeptidase II'', ''pyroglutamyl peptidase II'', ''thyroliberin-hydrolyzing pyro ... enzyme, that in humans is encoded by the TRHDE gene. Function This gene encodes a member of the peptidase M1 family. The encoded protein is an extracellular peptidase that specifically cleaves and inactivates the neuropeptide thyrotropin-releasing hormone. References Further reading * * * * * Genes on human chromosome 12 {{gene-12-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pyroglutamyl-peptidase II
Pyroglutamyl-peptidase II (, ''thyroliberinase'', ''pyroglutamyl aminopeptidase II'', ''thyrotropin-releasing factor pyroglutamate aminopeptidase'', ''pyroglutamate aminopeptidase II'', ''pyroglutamyl peptidase II'', ''thyroliberin-hydrolyzing pyroglutamate aminopeptidase'', ''thyrotropin-releasing hormone-degrading pyroglutamate aminopeptidase'', ''thyrotropin-releasing hormone-degrading peptidase'', ''TRH aminopeptidase'') is an enzyme. This enzyme catalyses the following chemical reaction : Release of the N-terminal pyroglutamyl group from pGlu--His-Xaa tripeptides and pGlu--His-Xaa-Gly tetrapeptides This enzyme is highly specific for thyrotropin releasing hormone Thyrotropin-releasing hormone (TRH) is a hypophysiotropic hormone produced by neurons in the hypothalamus that stimulates the release of thyroid-stimulating hormone (TSH) and prolactin from the anterior pituitary. TRH has been used clinicall .... Human gene TRHDE - thyrotropin releasing hormone degrading e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid resid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gene
In biology, the word gene (from , ; "... Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a basic unit of heredity and the molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protein-coding genes and noncoding genes. During gene expression, the DNA is first copied into RNA. The RNA can be directly functional or be the intermediate template for a protein that performs a function. The transmission of genes to an organism's offspring is the basis of the inheritance of phenotypic traits. These genes make up different DNA sequences called genotypes. Genotypes along with environmental and developmental factors determine what the phenotypes will be. Most biological traits are under the influence of polygenes (many different genes) as well as g ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptidase
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes (increases reaction rate or "speeds up") proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in many biological functions, including digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling. In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Hierarchy of proteases Based on catalytic residue Proteases can be classified into seven broad groups: * Serine pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Neuropeptide
Neuropeptides are chemical messengers made up of small chains of amino acids that are synthesized and released by neurons. Neuropeptides typically bind to G protein-coupled receptors (GPCRs) to modulate neural activity and other tissues like the gut, muscles, and heart. There are over 100 known neuropeptides, representing the largest and most diverse class of signaling molecules in the nervous system. Neuropeptides are synthesized from large precursor proteins which are cleaved and post-translationally processed then packaged into dense core vesicles. Neuropeptides are often co-released with other neuropeptides and neurotransmitters in a single neuron, yielding a multitude of effects. Once released, neuropeptides can diffuse widely to affect a broad range of targets. Synthesis Neuropeptides are synthesized from large, inactive precursor proteins called prepropeptides. Prepropeptides contain sequences for a family of distinct peptides and often contain repeated copies of the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thyrotropin-releasing Hormone
Thyrotropin-releasing hormone (TRH) is a hypophysiotropic hormone produced by neurons in the hypothalamus that stimulates the release of thyroid-stimulating hormone (TSH) and prolactin from the anterior pituitary. TRH has been used clinically for the treatment of spinocerebellar degeneration and disturbance of consciousness in humans. Its pharmaceutical form is called protirelin (INN) (). Synthesis and release TRH is synthesized within parvocellular neurons of the paraventricular nucleus of the hypothalamus. It is translated as a 242-amino acid precursor polypeptide that contains 6 copies of the sequence -Gln-His-Pro-Gly-, flanked by Lys-Arg or Arg-Arg sequences. To produce the mature form, a series of enzymes are required. First, a protease cleaves to the C-terminal side of the flanking Lys-Arg or Arg-Arg. Second, a carboxypeptidase removes the Lys/Arg residues leaving Gly as the C-terminal residue. Then, this Gly is converted into an amide residue by a series of enzym ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
