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Showing 11 - 20 of 110297 pathways
PathBank ID Pathway Chemical Compounds Proteins

SMP0002345

Pw002433 View Pathway
Metabolite

Xylitol Degradation

Saccharomyces cerevisiae
The degradation of xylose begins with NADP dependent trifunctional aldehyde reductase/xylose reductase/glucose 1-dehydrogenase resulting in the release of a NADPH, hydrogen ion and Xylitol. Xylitol reacts with a NAD D-xylulose reductase resulting in the release of NADH, a hydrogen ion and D-xylulose. Xylulose reacts with ATP through a xylulose kinase resulting in a release of ADP, hydrogen ion and xylulose 5-phosphate. The latter compound, xylulose 5-phosphate through a Ribulose-phosphate 3-epimerase resulting in the release of D-ribulose 5-phosphate. D-ribulose 5-phosphate and xylulose 5-phosphate react with a transketolase resulting in the release of D-glyceraldehyde 3-phosphate and D-sedoheptulose 7-phosphate. These two compounds react through a transaldolase resulting in the release of a D-erythrose 4-phosphate and Beta-D-fructofuranose 6-phosphate. D-erythrose 4-phosphate reacts with a xylulose 5-phosphate through a transketolase resulting in the release of Beta-D-fructofuranose 6-phosphate and D-glyceraldehyde 3-phosphate

Metabolic

SMP0122466

Pw123776 View Pathway
Metabolite

Xylene and Toluene Degradation

Pseudomonas aeruginosa
Xylene is a common aromatic hydrocarbon used in the medical industry as a solvent. This pathway describes a part of how xylene is degraded in certain bacterial species. Xylene exists in different percentages in a laboratory-grade level and is of a few common kinds: m-xylene (40–65%), p-xylene (20%), o-xylene (20%) and ethylbenzene (6-20%) and traces of toluene, trimethyl benzene, phenol, thiophene, pyridine, and hydrogen sulfide. In the bigger picture of this pathway, m-xylene, p-xylene, o-xylene as well as toluene are considered, where part of the degradation processes for each of these xylene types have been illustrated. All degradation reactions here are taking place in the cytoplasm. One part of this pathway starts with 4-methylbenzoic acid / p-methylbenzoate which is a product downstream of the p-xylene degradation and forms other intermediates: cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate, 4-methylcatechol, 3-methyl-cis,cis-muconate, 4-methylmuconolactone and 3-methylmuconolactone aided by the proteins and protein complexes: toluate-1,2-deoxygenase alpha and beta subunit, cis-1,2-dihydroxycyclohexa-3,4-diene carboxylate dehydrogenase, catechol 1,2-dioxygenase, and muconate cycloisomerase I. It must be noted that the intermediate 3-methyl-cis,cis-muconate gives rise to two products in this pathway via two different reactions using the same protein muconate cycloisomerase I. The other section of this pathway demonstrates the degradation of o-methylbenzoate and m-methylbenzoate. o-Methylbenzoae degrades down to the intermediate 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate and m-methylbenzoate degrades down to the intermediate 1,2-dihydroxy-3-methylcyclohexa-3,5-dienecarboxylate. They both then degrade to the same product/intermediate 3-methylcatechol. These reactions are both catalyzed by the proteins probable ring-hydroxylating dioxygenase subunit and cis-1,2-dihydroxycyclohexa-3,4-diene carboxylate dehydrogenase respectively.

Metabolic

SMP0000279

Pw000301 View Pathway
Metabolite

Ximelagatran Action Pathway

Homo sapiens
Ximelagatran is an anticoagulant drug used to prevent and treat blood clots, and was the first drug in the anticoagulant drug class to be able to be ingested orally. It was discontinued from distribution by its parent company AstraZeneca in 2006 as it was found to raise liver enzyme levels in patients and cause liver damage as a result. Ximelagatran inhibits prothrombin. Then zooming in even further to the endoplasmic reticulum within the liver, vitamin K1 2,3-epoxide uses vitamin K epoxide reductase complex subunit 1 to become reduced vitamin K (phylloquinone), and then back to vitamin K1 2,3-epoxide continually through vitamin K-dependent gamma-carboxylase. This enzyme also catalyzes precursors of prothrombin and coagulation factors VII, IX and X to prothrombin, and coagulation factors VII, IX and X. From there, these precursors and factors leave the liver cell and enter into the blood capillary bed. Once there, prothrombin is inhibited by ximelagatran, and is catalyzed into the protein complex prothrombinase complex which is made up of coagulation factor Xa/coagulation factor Va (platelet factor 3). These factors are joined by coagulation factor V and ximelagatran inhibits prothrombin. Through the two factors coagulation factor Xa and coagulation factor Va, thrombin is produced and inhibited by ximelagatran, which then uses fibrinogen alphabet, and gamma chains to create fibrin (loose). This is then turned into coagulation factor XIIIa, which is activated through coagulation factor XIII A and B chains. From here, fibrin (mesh) is produced which interacts with endothelial cells to cause coagulation. Plasmin is then created from fibrin (mesh), then joined by tissue-type plasminogen activator through plasminogen and creates fibrin degradation products. These are enzymes that stay in your blood after your body has dissolved a blood clot. Coming back to the factors transported from the liver, coagulation factor X is catalyzed into a group of enzymes called the tenase complex: coagulation factor IX and coagulation factor VIIIa (platelet factor 3). This protein complex is also contributed to by coagulation factor VIII, which through prothrombin is catalyzed into coagulation factor VIIIa. Prothrombin is inhibited by ximelagatran here as well. From there, this protein complex is catalyzed into prothrombinase complex, the group of proteins mentioned above, contributing to the above process ending in fibrin degradation products. Another enzyme transported from the liver is coagulation factor IX which becomes coagulation factor IXa, part of the tense complex, through coagulation factor XIa. Coagulation factor XIa is produced through coagulation factor XIIa which converts coagulation XI to become coagulation factor XIa. Coagulation factor XIIa is introduced through chain of activation starting in the endothelial cell with collagen alpha-1 (I) chain, which paired with coagulation factor XII activates coagulation factor XIIa. It is also activated through plasma prekallikrein and coagulation factor XIIa which activate plasma kallikrein, which then pairs with coagulation factor XII simultaneously with the previous collagen chain pairing to activate coagulation XIIa. Lastly, the previously transported coagulation factor VII and tissue factor coming from a vascular injury work together to activate tissue factor: coagulation factor VIIa. This enzyme helps coagulation factor X catalyze into coagulation factor Xa, to contribute to the prothrombinase complex and complete the pathway.

Drug Action

SMP0012035

Pw012896 View Pathway
Metabolite

Xanthophyll Cycle

Arabidopsis thaliana
Xanthophyll cycle is a pathway that transforms zeaxanthin to violaxanthin and antheraxanthin through enzymes. Xanthophyll cycle mainly takes place in diatoms and dinoflagellates of plants in high-light condition. Zeaxanthin is obatined from zeaxanthin biosynthesis that transforms lycopene to zeaxanthin (indirectly). Zeaxanthin is catalyzed into antheraxanthin and antheraxanthin catalyzed into violaxanthin both by the enzyme, zeaxanthin epoxidase with cofactor FAD. Violaxanthin deepoxidase/antheraxanthin deepoxidase can reverse the above reactions (i.e. violaxanthin to antheraxanthin and antheraxanthin to zeaxanthin).

Metabolic

SMP0120797

Pw122058 View Pathway
Metabolite

Xanthinuria Type II

Rattus norvegicus
Xanthinuria Type II is a rare inborn error of metabolism (IEM) and autosomal recessive disorder and caused by a defective xanthine dehydrogenase. Xanthine dehydrogenase catalyzes the conversion of hypoxanthine into xanthine and conversion of xanthine into uric acid. This disorder is characterized by a large accumulation of xanthine and hypoxanthine; as well as dissipation of uric acid. Symptoms of the disorder include blood in the urine, recurrent urinary tract infections and abdominal pain. It is estimated that xanthinuria types I and II affects 1 in 69,000 individuals.

Disease

SMP0120578

Pw121834 View Pathway
Metabolite

Xanthinuria Type II

Mus musculus
Xanthinuria Type II is a rare inborn error of metabolism (IEM) and autosomal recessive disorder and caused by a defective xanthine dehydrogenase. Xanthine dehydrogenase catalyzes the conversion of hypoxanthine into xanthine and conversion of xanthine into uric acid. This disorder is characterized by a large accumulation of xanthine and hypoxanthine; as well as dissipation of uric acid. Symptoms of the disorder include blood in the urine, recurrent urinary tract infections and abdominal pain. It is estimated that xanthinuria types I and II affects 1 in 69,000 individuals.

Disease

SMP0000513

Pw000489 View Pathway
Metabolite

Xanthinuria Type II

Homo sapiens
Xanthinuria Type II is a rare inborn error of metabolism (IEM) and autosomal recessive disorder and caused by a defective xanthine dehydrogenase. Xanthine dehydrogenase catalyzes the conversion of hypoxanthine into xanthine and conversion of xanthine into uric acid. This disorder is characterized by a large accumulation of xanthine and hypoxanthine; as well as dissipation of uric acid. Symptoms of the disorder include blood in the urine, recurrent urinary tract infections and abdominal pain. It is estimated that xanthinuria types I and II affects 1 in 69,000 individuals.

Disease

SMP0000512

Pw000488 View Pathway
Metabolite

Xanthinuria Type I

Homo sapiens
Xanthinuria Type I is a condition caused by an autosomal recessive mutation. The condition was discovered (though not diagnosed) in 1817, when stones formed of almost pure xanthine were first identified by Marcet. The symptoms arise because of a malfunction in the production of xanthine oxidase. It is a rare . It is characterized by a loss of oxidase such as in serum and the uric acid found in peepee. As a result, the opposite is true for the presence of xanthine and hypoxanthine. They will be found in the latter and former in increased quantities. Although the condition can cause a wide range of symptoms including renal xanthine stones, what occurs most of the time is that xanthinuria is asymptomatic and diagnosis is product of chance.

Disease

SMP0120796

Pw122057 View Pathway
Metabolite

Xanthinuria Type I

Rattus norvegicus
Xanthinuria Type I is a condition caused by an autosomal recessive mutation. The condition was discovered (though not diagnosed) in 1817, when stones formed of almost pure xanthine were first identified by Marcet. The symptoms arise because of a malfunction in the production of xanthine oxidase. It is a rare . It is characterized by a loss of oxidase such as in serum and the uric acid found in peepee. As a result, the opposite is true for the presence of xanthine and hypoxanthine. They will be found in the latter and former in increased quantities. Although the condition can cause a wide range of symptoms including renal xanthine stones, what occurs most of the time is that xanthinuria is asymptomatic and diagnosis is product of chance.

Disease

SMP0120577

Pw121833 View Pathway
Metabolite

Xanthinuria Type I

Mus musculus
Xanthinuria Type I is a condition caused by an autosomal recessive mutation. The condition was discovered (though not diagnosed) in 1817, when stones formed of almost pure xanthine were first identified by Marcet. The symptoms arise because of a malfunction in the production of xanthine oxidase. It is a rare . It is characterized by a loss of oxidase such as in serum and the uric acid found in peepee. As a result, the opposite is true for the presence of xanthine and hypoxanthine. They will be found in the latter and former in increased quantities. Although the condition can cause a wide range of symptoms including renal xanthine stones, what occurs most of the time is that xanthinuria is asymptomatic and diagnosis is product of chance.

Disease
Showing 11 - 20 of 110297 pathways