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ARG2
Arginase, type II is an arginase protein that in humans is encoded by the ARG2 gene. Function Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exists ( types I and II, this enzyme) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type II isoform encoded by this gene, is located in the mitochondria and expressed in extra-hepatic tissues, especially kidney. The physiologic role of this isoform is poorly understood; it is thought to play a role in nitric oxide and polyamine metabolism. Transcript variants of the type II gene resulting from the use of alternative polyadenylation Polyadenylation is the addition of a poly(A) tail to an RNA transcript, typically a messenger RNA (mRNA). The poly(A) tail consists of multiple adenosine monophosphates; in other words, it is a stretch of RNA that has only adenine bases. In euk ... sites have ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Arginase
Arginase (, ''arginine amidinase'', ''canavanase'', ''L-arginase'', ''arginine transamidinase'') is a manganese-containing enzyme. The reaction catalyzed by this enzyme is: : arginine + H2O → ornithine + urea It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Structure and function Arginase belong to the ureohydrolase family of enzymes. Arginase catalyzes the fifth and final step in the urea cycle, a series of biochemical reactions in mammals during which the body disposes of harmful ammonia. Specifically, arginase converts L-arginine into L-ornithine and urea. Mammalian arginase is active as a trimer, but some bacterial arginases are hexameric. The enzyme requires a two-molecule metal cluster of manganese in order to maintain proper function. These Mn2+ ions coordinate with water, orienting and stabilizing the molecule and allowing water to act as a nucleophile and attack L-arginine, hydrolyzing it into ornithine and urea. In most mammals, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Arginase
Arginase (, ''arginine amidinase'', ''canavanase'', ''L-arginase'', ''arginine transamidinase'') is a manganese-containing enzyme. The reaction catalyzed by this enzyme is: : arginine + H2O → ornithine + urea It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Structure and function Arginase belong to the ureohydrolase family of enzymes. Arginase catalyzes the fifth and final step in the urea cycle, a series of biochemical reactions in mammals during which the body disposes of harmful ammonia. Specifically, arginase converts L-arginine into L-ornithine and urea. Mammalian arginase is active as a trimer, but some bacterial arginases are hexameric. The enzyme requires a two-molecule metal cluster of manganese in order to maintain proper function. These Mn2+ ions coordinate with water, orienting and stabilizing the molecule and allowing water to act as a nucleophile and attack L-arginine, hydrolyzing it into ornithine and urea. In most mammals, ... [...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 residue ... [...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 gen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Arginine
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the -arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid. History Arginine was first isolated in 1886 from yellow lupin seedlings by the German chemist Ernst Schulze and his assistant Ernst Steiger. He named it from the Greek ''árgyros'' (ἄργυρος) meaning "silver" due to the silver-white appearance of arginine nitrate crystals. In 1897, Schulze and Ernst Winterstein (1865–1949) determined the structure ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ornithine
Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl. Role in urea cycle L-Ornithine is one of the products of the action of the enzyme arginase on L-arginine, creating urea. Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen. Ornithine is recycled and, in a manner, is a catalyst. First, ammonia is converted into carbamoyl phosphate (). Ornithine is converted into a urea derivative at the δ (terminal) nitrogen by carbamoyl phosphate synthetase. Another nitrogen is added from aspartate, producing the denitrogenated fumarate, and the resulting arginine (a guanidinium compound) is hydrolysed back to ornithine, producing urea. The nitrogens of urea come from the ammonia and aspartate, and the nitrogen in ornithine remains intact. Ornithine is not an amino acid coded for by DNA, that is, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Urea
Urea, also known as carbamide, is an organic compound with chemical formula . This amide has two amino groups (–) joined by a carbonyl functional group (–C(=O)–). It is thus the simplest amide of carbamic acid. Urea serves an important role in the metabolism of nitrogen-containing compounds by animals and is the main nitrogen-containing substance in the urine of mammals. It is a colorless, odorless solid, highly soluble in water, and practically non-toxic ( is 15 g/kg for rats). Dissolved in water, it is neither acidic nor alkaline. The body uses it in many processes, most notably nitrogen excretion. The liver forms it by combining two ammonia molecules () with a carbon dioxide () molecule in the urea cycle. Urea is widely used in fertilizers as a source of nitrogen (N) and is an important raw material for the chemical industry. In 1828 Friedrich Wöhler discovered that urea can be produced from inorganic starting materials, which was an important conceptual milestone ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ARG1
The human ARG1 gene encodes the protein arginase. Function Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform encoded by this gene, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia Hyperammonemia is a metabolic disturbance characterised by an excess of ammonia in the blood. It is a dangerous condition that may lead to brain injury and death. It may be primary or secondary. Ammonia is a substance that contains nitrogen. It i .... Two transcript variants encoding different isoforms have been found for this gene. rovided by RefSeq, Sep 2011/ref> References External links * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitric Oxide
Nitric oxide (nitrogen oxide or nitrogen monoxide) is a colorless gas with the formula . It is one of the principal oxides of nitrogen. Nitric oxide is a free radical: it has an unpaired electron, which is sometimes denoted by a dot in its chemical formula In chemistry, a chemical formula is a way of presenting information about the chemical proportions of atoms that constitute a particular chemical compound or molecule, using chemical element symbols, numbers, and sometimes also other symbols, ... (•N=O or •NO). Nitric oxide is also a heteronuclear diatomic molecule, a class of molecules whose study spawned early modern molecular orbital theory, theories of chemical bonding. An important Reaction intermediate, intermediate in chemical industry, industrial chemistry, nitric oxide forms in combustion systems and can be generated by lightning in thunderstorms. In mammals, including humans, nitric oxide is a signaling molecule in many physiological and pathological pro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polyamine
A polyamine is an organic compound having more than two amino groups. Alkyl polyamines occur naturally, but some are synthetic. Alkylpolyamines are colorless, hygroscopic, and water soluble. Near neutral pH, they exist as the ammonium derivatives. Most aromatic polyamines are crystalline solids at room temperature. Natural polyamines Low-molecular-weight linear polyamines are found in all forms of life. The principal examples are the triamine spermidine and the tetraamine spermine. They are structurally and biosynthetically related to the diamines putrescine and cadaverine. Polyamine metabolism is regulated by the activity of the enzyme ornithine decarboxylase (ODC). Polyamines are found in high concentrations in the mammalian brain. File:Spermidine-2D-skeletal.svg, spermidine File:Spermine.svg, spermine Synthetic polyamines Several synthetic polyamines are used in chemical industry and the research laboratory. They are mainly of interest as additives to motor oil and as co-rea ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polyadenylation
Polyadenylation is the addition of a poly(A) tail to an RNA transcript, typically a messenger RNA (mRNA). The poly(A) tail consists of multiple adenosine monophosphates; in other words, it is a stretch of RNA that has only adenine bases. In eukaryotes, polyadenylation is part of the process that produces mature mRNA for translation. In many bacteria, the poly(A) tail promotes degradation of the mRNA. It, therefore, forms part of the larger process of gene expression. The process of polyadenylation begins as the transcription of a gene terminates. The 3′-most segment of the newly made pre-mRNA is first cleaved off by a set of proteins; these proteins then synthesize the poly(A) tail at the RNA's 3′ end. In some genes these proteins add a poly(A) tail at one of several possible sites. Therefore, polyadenylation can produce more than one transcript from a single gene (alternative polyadenylation), similar to alternative splicing. The poly(A) tail is important for the nuclea ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
