PathWhiz

PathWhiz ID	Pathway	Meta Data
PW000811 View Pathway	metabolic Leucine Biosynthesis Escherichia coli Leucine biosynthesis involves a five-step conversion process starting with the valine precursor 2-keto-isovalerate interacting with acetyl-CoA and water through a 2-isopropylmalate synthase resulting in Coenzyme A, hydrogen Ion and 2-isopropylmalic acid. The latter compound reacts with isopropylmalate isomerase which dehydrates the compound resulting in a Isopropylmaleate. This compound reacts with water through a isopropylmalate isomerase resulting in 3-isopropylmalate. This compound interacts with a NAD-driven D-malate / 3-isopropylmalate dehydrogenase results in 2-isopropyl-3-oxosuccinate. This compound interacts spontaneously with hydrogen resulting in the release of carbon dioxide and ketoleucine. Ketoleucine interacts in a reversible reaction with L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in Oxoglutaric acid and L-leucine. L-leucine can then be exported outside the cytoplasm through a transporter: L-amino acid efflux transporter. In the final step, ketoleucine can be catalyzed to form L-leucine by branched-chain amino-acid aminotransferase (IlvE) and tyrosine aminotransferase (TryB). L-Glutamic acid can also be transformed into oxoglutaric acid by these two enzymes. Tyrosine aminotransferase can be suppressed by lecuine, and inhibited by 2-keto-isovarlerate and its end product, tyrosine. 2-ketoisocaproate can not be introduced if 2-keto-isovarlerate inhibit TyrB and IlvE is absent. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: miguel ramirez Created On: March 16, 2015 at 15:51 Last Updated: March 16, 2015 at 15:51
PW122595 View Pathway	metabolic Leucine Biosynthesis Pseudomonas aeruginosa Leucine biosynthesis involves a five-step conversion process starting with the valine precursor 2-keto-isovalerate interacting with acetyl-CoA and water through a 2-isopropylmalate synthase resulting in Coenzyme A, hydrogen Ion and 2-isopropylmalic acid. The latter compound reacts with isopropylmalate isomerase which dehydrates the compound resulting in a Isopropylmaleate. This compound reacts with water through a isopropylmalate isomerase resulting in 3-isopropylmalate. This compound interacts with a NAD-driven D-malate / 3-isopropylmalate dehydrogenase results in 2-isopropyl-3-oxosuccinate. This compound interacts spontaneously with hydrogen resulting in the release of carbon dioxide and ketoleucine. Ketoleucine interacts in a reversible reaction with L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in Oxoglutaric acid and L-leucine. L-leucine can then be exported outside the cytoplasm through a transporter: L-amino acid efflux transporter. In the final step, ketoleucine can be catalyzed to form L-leucine by branched-chain amino-acid aminotransferase (IlvE) and tyrosine aminotransferase (TryB). L-Glutamic acid can also be transformed into oxoglutaric acid by these two enzymes. Tyrosine aminotransferase can be suppressed by lecuine, and inhibited by 2-keto-isovarlerate and its end product, tyrosine. 2-ketoisocaproate can not be introduced if 2-keto-isovarlerate inhibit TyrB and IlvE is absent. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ana Marcu Created On: August 12, 2019 at 18:20 Last Updated: August 12, 2019 at 18:20
PW002540 View Pathway	metabolic Leucine Biosynthesis Arabidopsis thaliana Leucine biosynthesis involves a five-step conversion process starting with the valine precursor 2-keto-isovalerate interacting with acetyl-CoA and water through a 2-isopropylmalate synthase resulting in Coenzyme A, hydrogen Ion and 2-isopropylmalic acid. The latter compound reacts with isopropylmalate isomerase which dehydrates the compound resulting in a Isopropylmaleate. This compound reacts with water through a isopropylmalate isomerase resulting in 3-isopropylmalate. This compound interacts with a NAD-driven D-malate / 3-isopropylmalate dehydrogenase results in 2-isopropyl-3-oxosuccinate. This compound interacts spontaneously with hydrogen resulting in the release of carbon dioxide and ketoleucine. Ketoleucine interacts in a reversible reaction with L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in Oxoglutaric acid and L-leucine. L-leucine can then be exported outside the cytoplasm through a transporter: L-amino acid efflux transporter. In the final step, ketoleucine can be catalyzed to form L-leucine by branched-chain amino-acid aminotransferase (IlvE) and tyrosine aminotransferase (TryB). L-Glutamic acid can also be transformed into oxoglutaric acid by these two enzymes. Tyrosine aminotransferase can be suppressed by lecuine, and inhibited by 2-keto-isovarlerate and its end product, tyrosine. 2-ketoisocaproate can not be introduced if 2-keto-isovarlerate inhibit TyrB and IlvE is absent. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: miguel ramirez Created On: May 05, 2016 at 14:53 Last Updated: May 05, 2016 at 14:53
PW002475 View Pathway	metabolic Leucine Biosynthesis Saccharomyces cerevisiae Leucine biosynthesis involves a five-step conversion process starting with the valine precursor 2-keto-isovalerate interacting with acetyl-CoA and water through a 2-isopropylmalate synthase resulting in Coenzyme A, hydrogen Ion and 2-isopropylmalic acid. The latter compound reacts with isopropylmalate isomerase which dehydrates the compound resulting in a Isopropylmaleate. This compound reacts with water through a isopropylmalate isomerase resulting in 3-isopropylmalate. This compound interacts with a NAD-driven D-malate / 3-isopropylmalate dehydrogenase results in 2-isopropyl-3-oxosuccinate. This compound interacts spontaneously with hydrogen resulting in the release of carbon dioxide and ketoleucine. Ketoleucine interacts in a reversible reaction with L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in Oxoglutaric acid and L-leucine. L-leucine can then be exported outside the cytoplasm through a transporter: L-amino acid efflux transporter. In the final step, ketoleucine can be catalyzed to form L-leucine by branched-chain amino-acid aminotransferase (IlvE) and tyrosine aminotransferase (TryB). L-Glutamic acid can also be transformed into oxoglutaric acid by these two enzymes. Tyrosine aminotransferase can be suppressed by lecuine, and inhibited by 2-keto-isovarlerate and its end product, tyrosine. 2-ketoisocaproate can not be introduced if 2-keto-isovarlerate inhibit TyrB and IlvE is absent. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: miguel ramirez Created On: February 19, 2016 at 13:35 Last Updated: February 19, 2016 at 13:35
PW013301 View Pathway	metabolic Leucine degradation Bacteria I would like to test Pathwhiz BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Guest: Anonymous Created On: April 27, 2017 at 06:57 Last Updated: April 27, 2017 at 06:57
PW002490 View Pathway	metabolic Leucine Degradation Saccharomyces cerevisiae The degradation of L-leucine starts either in the mitochondria or the cytosol. L-leucine reacts with 2-oxoglutarate through a branch-chain amino acid aminotransferase resulting in the release of ketoleucine and glutamate. The latter compound reacts with ketoisocaproate decarboxylase resulting in the release of carbon dioxide and 3-methylbutanal. The latter compound can then be turned into 3-methylbutanol through a alcohol dehydrogenase BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: miguel ramirez Created On: February 29, 2016 at 14:20 Last Updated: February 29, 2016 at 14:20
PW002541 View Pathway	metabolic Leucine Degradation Arabidopsis thaliana The degradation of L-leucine starts either in the mitochondria, the cytosol or the chloroplast. L-leucine reacts with 2-oxoglutarate through a branch-chain amino acid aminotransferase resulting in the release of ketoleucine and glutamate. Ketoleucine reacts with coenzyme a through a NAD dependent branched chain keto-acid dehydrogenase complex resulting in the release of NADH, carbon dioxide and isovaleryl-CoA. Isovaleryl-CoA reacts with an oxidized electron flavoprotein resulting in the release of a reduced flavoprotein and a methylcrotonyl-CoA. The latter reacts with ATP and hydrogen carbonate through a 3-methylcrotonyl-CoA carboxylase resulting in the release of phosphate, ADP, hydrogen ion and 3-methylglutaconyl-CoA. The latter compound reacts with water through a methylglutaconyl-CoA hydratase resulting in the release of hydroxy-3-methylglutaryl-CoA. The latter reacts with a hydroxymethylglutaryl-CoA lyase resulting in the release of acetyl-CoA and acetoacetate. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: miguel ramirez Created On: May 05, 2016 at 16:47 Last Updated: May 05, 2016 at 16:47
PW109051 View Pathway	signaling Leucine Stimulation on Insulin Signaling Rattus norvegicus The branched chain amino acid (BCAA) leucine is able to signal transduction pathways that modulate translation initiation for protein synthesis in skeleton muscles. In the presence of leucine, hyperphosphorylation of 4E-BP1 causes its affinity for eIF4E to be lowered. This allows eIF4F protein complexes to recognize, unfold and guide the mRNA to the 43S preinitiation complex thereby increasing translation initiation. In addition, leucine has a transient affect on the release of insulin and/or enhances sensitivity of muscle cells to insulin. A culmination of both signals at the mammalian target of rapamycin (mTOR) and perhaps other signaling, such as PKCδ, are needed for maximum translation initiation to occur. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ana Marcu Created On: August 31, 2018 at 11:46 Last Updated: August 31, 2018 at 11:46
PW109041 View Pathway	signaling Leucine Stimulation on Insulin Signaling Bos taurus The branched chain amino acid (BCAA) leucine is able to signal transduction pathways that modulate translation initiation for protein synthesis in skeleton muscles. In the presence of leucine, hyperphosphorylation of 4E-BP1 causes its affinity for eIF4E to be lowered. This allows eIF4F protein complexes to recognize, unfold and guide the mRNA to the 43S preinitiation complex thereby increasing translation initiation. In addition, leucine has a transient affect on the release of insulin and/or enhances sensitivity of muscle cells to insulin. A culmination of both signals at the mammalian target of rapamycin (mTOR) and perhaps other signaling, such as PKCδ, are needed for maximum translation initiation to occur. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ana Marcu Created On: August 31, 2018 at 11:45 Last Updated: August 31, 2018 at 11:45
PW109030 View Pathway	signaling Leucine Stimulation on Insulin Signaling Mus musculus The branched chain amino acid (BCAA) leucine is able to signal transduction pathways that modulate translation initiation for protein synthesis in skeleton muscles. In the presence of leucine, hyperphosphorylation of 4E-BP1 causes its affinity for eIF4E to be lowered. This allows eIF4F protein complexes to recognize, unfold and guide the mRNA to the 43S preinitiation complex thereby increasing translation initiation. In addition, leucine has a transient affect on the release of insulin and/or enhances sensitivity of muscle cells to insulin. A culmination of both signals at the mammalian target of rapamycin (mTOR) and perhaps other signaling, such as PKCδ, are needed for maximum translation initiation to occur. BioPAX SVG SBGN SBML PWML All files (.zip)	Creator: Ana Marcu Created On: August 31, 2018 at 11:43 Last Updated: August 31, 2018 at 11:43