PathWhiz

PathWhiz ID	Pathway	Meta Data
PW088222 View Pathway	metabolic Lysine Degradation Bos taurus The degradation of L-lysine happens in liver and it is consisted of seven reactions. L-Lysine is imported into liver through low affinity cationic amino acid transporter 2 (cationic amino acid transporter 2/SLC7A2). Afterwards, L-lysine is imported into mitochondria via mitochondrial ornithine transporter 2. L-Lysine can also be obtained from biotin metabolism. L-Lysine and oxoglutaric acid will be combined to form saccharopine by facilitation of mitochondrial alpha-aminoadipic semialdehyde synthase, and then, mitochondrial alpha-aminoadipic semialdehyde synthase will further breaks saccharopine down to allysine and glutamic acid. Allysine will be degraded to form aminoadipic acid through alpha-aminoadipic semialdehyde dehydrogenase. Oxoadipic acid is formed from catalyzation of mitochondrial kynurenine/alpha-aminoadipate aminotransferase on aminoadipic acid. Oxoadipic acid will be further catalyzed to form glutaryl-CoA, and glutaryl-CoA converts to crotonoyl-CoA, and crotonoyl-CoA transformed to 3-hydroxybutyryl-CoA. 3-Hydroxybutyryl-CoA will form Acetyl-CoA as the final product through the intermediate compound: acetoacetyl-CoA. Acetyl-CoA will undergo citric acid cycle metabolism. Carnitine is another key byproduct of lysine metabolism (not shown in this pathway). BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ana Marcu Created On: August 10, 2018 at 11:22 Last Updated: August 10, 2018 at 11:22
PW000772 View Pathway	metabolic Lysine Degradation Escherichia coli Lysine is an essential amino acid used in protein synthesis. Lysine can be transported into the cell by probable cadaverine (also known as lysine antiporter). Once inside the cell, lysine is decarboxylated by lysine decarboxylase to cadaverine. Cadaverine can then exit the cell via the same type of transporter as lysine (probable cadaverine). Alternatively, lysine can be produced during lysine biosynthesis (from aspartic acid) inside the cell and used in the same pathway. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: miguel ramirez Created On: February 08, 2015 at 16:11 Last Updated: February 08, 2015 at 16:11
PW122575 View Pathway	metabolic Lysine Degradation I Pseudomonas aeruginosa Lysine is an essential amino acid used in protein synthesis. Lysine can be transported into the cell by probable cadaverine (also known as lysine antiporter). Once inside the cell, lysine is decarboxylated by lysine decarboxylase to cadaverine. Cadaverine can then exit the cell via the same type of transporter as lysine (probable cadaverine). Alternatively, lysine can be produced during lysine biosynthesis (from aspartic acid) inside the cell and used in the same pathway. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ana Marcu Created On: August 12, 2019 at 16:59 Last Updated: August 12, 2019 at 16:59
PW144269 View Pathway	drug action Lysine Drug Metabolism Action Pathway Homo sapiens BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ray Kruger Created On: October 07, 2023 at 13:04 Last Updated: October 07, 2023 at 13:04
PW002420 View Pathway	metabolic Lysine Metabolism Saccharomyces cerevisiae The biosynthesis of lysine starts with oxoglutaric acid interacting with acetyl-coa through a homocitrate synthase resulting in the release of homocitric acid. This reaction may happen in the cytosol or in the mitochondria. The homocitric acid spontaneously releases water an is transformed into cis-homoaconitate, The cis-homoaconitate reacts with homoaconitase resulting in the release of water and a homoisocitrate. Homoisocitrate reacts with a NAD dependent homoisocitrate dehydrogenase resulting in the release of a carbon dioxide, a NADH and a oxoadipic acid. These set of reactions happen in the mitochondria. Oxoadipic acid reacts with a glutamic acid resulting in the release of oxoglutaric acid and aminoadipic acid. The aminoadipic acid reacts with a holo-[LYS2 peptidyl-carrier-protein] through an ATP driven L-2-aminoadipate reductase resulting in the release of AMP, pyrophosphate and L-2-aminoadipyl-[lys2 peptidyl-carrier-protein]. This resulting element reacts with a NADPH dependent L-2-aminoadipate reductase resulting in the release of allysine. Allysine reacts with a glutamic acid through a NADPH dependent saccharopine dehydrogenase resulting in the release of water, NADP and saccharopine. Saccharopine reacts with a water molecule and a NAD dependent saccharopine dehydrogenase resulting in the release of oxoglutaric acid and L-lysine. This last reaction is reversible and leads to the degradation of lysine BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: miguel ramirez Created On: January 19, 2016 at 10:36 Last Updated: January 19, 2016 at 10:36
PW002543 View Pathway	metabolic Lysine Metabolism Arabidopsis thaliana The biosynthesis of lysine starts with oxoglutaric acid interacting with acetyl-coa through a homocitrate synthase resulting in the release of homocitric acid. This reaction may happen in the cytosol or in the mitochondria. The homocitric acid spontaneously releases water an is transformed into cis-homoaconitate, The cis-homoaconitate reacts with homoaconitase resulting in the release of water and a homoisocitrate. Homoisocitrate reacts with a NAD dependent homoisocitrate dehydrogenase resulting in the release of a carbon dioxide, a NADH and a oxoadipic acid. These set of reactions happen in the mitochondria. Oxoadipic acid reacts with a glutamic acid resulting in the release of oxoglutaric acid and aminoadipic acid. The aminoadipic acid reacts with a holo-[LYS2 peptidyl-carrier-protein] through an ATP driven L-2-aminoadipate reductase resulting in the release of AMP, pyrophosphate and L-2-aminoadipyl-[lys2 peptidyl-carrier-protein]. This resulting element reacts with a NADPH dependent L-2-aminoadipate reductase resulting in the release of allysine. Allysine reacts with a glutamic acid through a NADPH dependent saccharopine dehydrogenase resulting in the release of water, NADP and saccharopine. Saccharopine reacts with a water molecule and a NAD dependent saccharopine dehydrogenase resulting in the release of oxoglutaric acid and L-lysine. This last reaction is reversible and leads to the degradation of lysine BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: miguel ramirez Created On: May 06, 2016 at 16:44 Last Updated: May 06, 2016 at 16:44
PW000220 View Pathway	disease Lysinuric Protein Intolerance Homo sapiens Lysinuric protein intolerance (Hyperdibasic aminoaciduria II; Dibasic aminoaciduria II; Hyperdibasic aminoaciduria II; LPI), also called hyperdibasic aminoaciduria type 2 or familial protein intolerance, is an autosomal recessive metabolic disorder affecting amino acid transport. LPI is caused by a defect in SLC7A7, Solute carrier family 7, a cationic amino acid transporter. A defect in this enzyme results in accumulation of ammmonia and reticulocytes in blood; glutamine in plasma, carnitine and ferritin in serum, and arginine, lysine and ornithine in urine. Symptoms include bone marrow abnormality, growth retardation, hyperammoniemia, mental retardation, pancreatitis, and seizures. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: WishartLab Created On: August 20, 2013 at 15:20 Last Updated: August 20, 2013 at 15:20
PW121804 View Pathway	disease Lysinuric Protein Intolerance Mus musculus Lysinuric protein intolerance (Hyperdibasic aminoaciduria II; Dibasic aminoaciduria II; Hyperdibasic aminoaciduria II; LPI), also called hyperdibasic aminoaciduria type 2 or familial protein intolerance, is an autosomal recessive metabolic disorder affecting amino acid transport. LPI is caused by a defect in SLC7A7, Solute carrier family 7, a cationic amino acid transporter. A defect in this enzyme results in accumulation of ammmonia and reticulocytes in blood; glutamine in plasma, carnitine and ferritin in serum, and arginine, lysine and ornithine in urine. Symptoms include bone marrow abnormality, growth retardation, hyperammoniemia, mental retardation, pancreatitis, and seizures. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ana Marcu Created On: September 10, 2018 at 15:49 Last Updated: September 10, 2018 at 15:49
PW122029 View Pathway	disease Lysinuric Protein Intolerance Rattus norvegicus Lysinuric protein intolerance (Hyperdibasic aminoaciduria II; Dibasic aminoaciduria II; Hyperdibasic aminoaciduria II; LPI), also called hyperdibasic aminoaciduria type 2 or familial protein intolerance, is an autosomal recessive metabolic disorder affecting amino acid transport. LPI is caused by a defect in SLC7A7, Solute carrier family 7, a cationic amino acid transporter. A defect in this enzyme results in accumulation of ammmonia and reticulocytes in blood; glutamine in plasma, carnitine and ferritin in serum, and arginine, lysine and ornithine in urine. Symptoms include bone marrow abnormality, growth retardation, hyperammoniemia, mental retardation, pancreatitis, and seizures. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ana Marcu Created On: September 10, 2018 at 15:51 Last Updated: September 10, 2018 at 15:51
PW000561 View Pathway	disease Lysinuric Protein Intolerance (LPI) Homo sapiens Lysinuric protein intolerance (LPI), also called hyperdibasic aminoaciduria, is a rare inborn error of metabolism (IEM) and autosomal recessive disorder of the kidney function pathway. It is caused by a mutation in the SLC7A7 gene which encodes the Y+L amino acid transporter 1 protein, which is involved in the uptake of amino acids, both with sodium for neutral amino acids, and without for dibasic amino acids. In this disorder, the amino acids lysin, arginine and ornithine, found in protein, cannot be broken down, which can cause problems in the systems that use these amino acids, such as the urea cycle. LPI is characterized by a shortage of lysine, arginine and ornithine within the body, causing elevated ammonia levels in the blood. Symptoms of the disorder include failure to thrive after weaning, nausea and vomiting following a meal containing large amounts of protein, as well as osteoporosis, and lung and kidney problems. Treatment with a protein restricted diet is effective, as well as prescription of medication to lower the levels of ammonia in the blood. It is estimated that the LPI affects 1 in 60,000 individuals in certain populations such as in Finland and Japan, and less frequently outside these populations. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: WishartLab Created On: August 29, 2013 at 10:39 Last Updated: August 29, 2013 at 10:39