OrnithineOrnithine decarboxylase: The enzyme ornithine decarboxylase (ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) to form putrescine. This reaction is the committed step in polyamine synthesis.N-succinylornithine carbamoyltransferase: N-succinylornithine carbamoyltransferase (, succinylornithine transcarbamylase, N-succinyl-L-ornithine transcarbamylase, SOTCase) is an enzyme with system name carbamoyl phosphate:N2-succinyl-L-ornithine carbamoyltransferase. This enzyme catalyses the following chemical reactionOrnithine aminotransferase deficiency: Ornithine aminotransferase deficiency (also known as gyrate atrophy of the choroid and retina) is an inborn error of ornithine metabolism, caused by decreased activity of the enzyme ornithine aminotransferase. Biochemically, it can be detected by elevated levels of ornithine in the blood.Ornithine transcarbamylase: Ornithine transcarbamylase (OTC) (also called ornithine carbamoyltransferase) is an enzyme that catalyzes the reaction between carbamoyl phosphate (CP) and ornithine (Orn) to form citrulline (Cit) and phosphate (Pi). In plants and microbes, OTC is involved in arginine (Arg) biosynthesis, whereas in mammals it is located in the mitochondria and is part of the urea cycle.EflornithinePutrescine aminotransferase: Putrescine aminotransferase (, putrescine-alpha-ketoglutarate transaminase, YgjG, putrescine:alpha-ketoglutarate aminotransferase, PAT, putrescine:2-oxoglutarate aminotransferase, putrescine transaminase) is an enzyme with system name butane-1,4-diamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reactionGroup IV pyridoxal-dependent decarboxylases: In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase , lysine decarboxylase , arginine decarboxylase and diaminopimelate decarboxylase. It is also known as the Orn/Lys/Arg decarboxylase class-II family.SpermidineCitrullineProtein detoxification: Protein detoxification is the process by which proteins containing methylated arginine are broken down and removed from the body.Adenosylmethionine decarboxylase: Adenosylmethionine decarboxylase is an enzyme that catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine.SpermineArginaseDiaminopropane: Diaminopropane may refer to either of two isomeric chemical compounds:Carbamoyl phosphatePhosphoserine transaminase: Phosphoserine transaminase (, PSAT, phosphoserine aminotransferase, 3-phosphoserine aminotransferase, hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine aminotransferase, phosphohydroxypyruvate transaminase, phosphohydroxypyruvic-glutamic transaminase, 3-O-phospho-L-serine:2-oxoglutarate aminotransferase, SerC, PdxC, 3PHP transaminase) is an enzyme with system name O-phospho-L-serine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reactionConstitutive enzyme: Constitutive enzymeshttp://goldbook.iupac.Carbamoyl phosphate synthetaseHyperammonemiaUrea reduction ratio: For the Scottish river see: Urr WaterProline-Rich Coiled Coil 1: Proline Rich Coiled Coil-1 (PRCC1) is the commonly identified protein name of CAD38605. The PRCC1 gene is found on the long arm of Chromosome 5.Decarboxylation: Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO2). Usually, decarboxylation refers to a reaction of carboxylic acids, removing a carbon atom from a carbon chain.Burst kinetics: Burst kinetics is a form of enzyme kinetics that refers to an initial high velocity of enzymatic turnover when adding enzyme to substrate. This initial period of high velocity product formation is referred to as the "Burst Phase".Tyrosine ammonia-lyase: Tyrosine ammonia lyase (L-tyrosine ammonia-lyase, TAL or Tyrase) is an enzyme in the natural phenols biosynthesis pathway. It transforms L-tyrosine into p-coumaric acid.Ammonia transporterProteinogenic amino acid: Proteinogenic amino acids are amino acids that are precursors to proteins, and are incorporated into proteins cotranslationally — that is, during translation. There are 23 proteinogenic amino acids in prokaryotes (including N-Formylmethionine, mainly used to initiate protein synthesis and often removed afterward), but only 21 are encoded by the nuclear genes of eukaryotes.MitoguazoneCadaverineLiver sinusoid: A liver sinusoid is a type of sinusoidal blood vessel (with fenestrated, discontinuous endothelium) that serves as a location for the oxygen-rich blood from the hepatic artery and the nutrient-rich blood from the portal vein.SIU SOM Histology GILysinuric protein intoleranceOrotic acidColes PhillipsGlutamineCyclohexylamineMature messenger RNA: Mature messenger RNA, often abbreviated as mature mRNA is a eukaryotic RNA transcript that has been spliced and processed and is ready for translation in the course of protein synthesis. Unlike the eukaryotic RNA immediately after transcription known as precursor messenger RNA, it consists exclusively of exons, with all introns removed.Ligase: In biochemistry, ligase (from the Latin verb ligāre — "to bind" or "to glue together") is an enzyme that can catalyze the joining of two large molecules by forming a new chemical bond, usually with accompanying hydrolysis of a small pendant chemical group on one of the larger molecules or the enzyme catalyzing the linking together of two compounds, e.g.AcetyllysineCycloheximideUreohydrolaseAcetyltransferaseMalonyl-S-ACP:biotin-protein carboxyltransferase: Malonyl-S-ACP:biotin-protein carboxyltransferase (, malonyl-S-acyl-carrier protein:biotin-protein carboxyltransferase, MadC/MadD, MadC,D, malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxyltransferase) is an enzyme with system name malonyl-(acyl-carrier protein):biotinyl-(protein) carboxytransferase. This enzyme catalyses the following chemical reactionProtein primary structure: The primary structure of a peptide or protein is the linear sequence of its amino acid structural units, and partly comprises its overall biomolecular structure. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end.Argininemia: Argininemia, also called arginase deficiency, is an autosomal recessive urea cycle disorder where a deficiency of the enzyme arginase causes a buildup of arginine and ammonia in the blood.Symmetry element: A symmetry element is a point of reference about which symmetry operations can take place. In particular, symmetry elements can be centers of inversion, axes of rotation and mirror planes.Cys/Met metabolism PLP-dependent enzyme family: In molecular biology, the Cys/Met metabolism PLP-dependent enzyme family is a family of proteins including enzymes involved in cysteine and methionine metabolism which use PLP (pyridoxal-5'-phosphate) as a cofactor.DNA condensation: DNA condensation refers to the process of compacting DNA molecules in vitro or in vivo. Mechanistic details of DNA packing are essential for its functioning in the process of gene regulation in living systems.Translational regulation: Translational regulation refers to the control of the levels of protein synthesized from its mRNA. The corresponding mechanisms are primarily targeted on the control of ribosome recruitment on the initiation codon, but can also involve modulation of the elongation or termination of protein synthesis.Silent mutation: Silent mutations are mutations in DNA that do not significantly alter the phenotype of the organism in which they occur. Silent mutations can occur in non-coding regions (outside of genes or within introns), or they may occur within exons.Phorbol 12,13-dibutyrateLaryngeal papillomatosisList of strains of Escherichia coli: Escherichia coli is a well studied bacterium that was first identified by Theodor Escherich, after whom it was later named.CrassaLigation-independent cloning: Ligation-independent cloning (LIC) is a form of molecular cloning that is able to be performed without the use of restriction endonucleases or DNA ligase. This allows genes that have restriction sites to be cloned without worry of chopping up the insert.Thermospermine synthase: Thermospermine synthase (, TSPMS, ACL5, SAC51) is an enzyme with system name S-adenosylmethioninamine:spermidine 3-aminopropyltransferase (thermospermine synthesizing). This enzyme catalyses the following chemical reactionMinC: The MinC protein is one of three proteins encoded by the minB operon and which is required to generate pole to pole oscillations prior to bacterial cell division as a means of specifying the midzone of the cell. This function is achieved by preventing the formation of the divisome Z-ring around the poles.Kidney: The kidneys are bean-shaped organs that serve several essential regulatory roles in vertebrates. They remove excess organic molecules from the blood, and it is by this action that their best-known function is performed: the removal of waste products of metabolism.Lattice protein: Lattice proteins are highly simplified computer models of proteins which are used to investigate protein folding.Jimson Weed (painting): Jimson Weed is an oil on linen painting by American artist Georgia O'Keeffe from 1936, located in the Indianapolis Museum of Art, which is in Indianapolis, Indiana, USA. It depicts four large blossoms of jimson weed, or datura.Arginine repressor ArgR: In molecular biology, the arginine repressor (ArgR) is a repressor of prokaryotic arginine deiminase pathways.Alkyne: In organic chemistry, an alkyne is an unsaturated hydrocarbon containing at least one carbon—carbon triple bond between two carbon atoms.Alkyne.
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