Pathways

Aminocaproic acid (also known as ε-aminocaproic acid, ε-Ahx, or 6-aminohexanoic acid; brand name Amicar) is a derivative of lysine, meaning that it acts as an amino acid analogue and can alter functionality of enzymes that require lysine residue binding (e.g. amino acid transporters such as the SLC3A2/SLC7A6 proteins, fibrin, tissue-type plasminogen activator, apolipoprotein(a), aldehyde oxidase, etc.). After oral or intravenous administration, it reaches the bloodstream and can act at the site of vascular injury (or other cause of excess bleeding) where the coagulation (i.e. blood clotting) takes place. Aminocaproic acid is an antifibrinolytic drug. Antifibrinolytics drugs are commonly used during major surgery to prevent significant blood loss (e.g. a liver transplant). By reversibly blocking the binding sites on plasminogen, aminocaproic acid creates a ‘blockade’ in the process of fibrinolysis - this blockade inhibits plasminogen binding to fibrin and the conversion of plasminogen to plasmin (a proteolytic enzyme), preventing fibrin degradation to maintain the stability of fibrin mesh/clots formed through the coagulation cascade. Thus, it reduces clot breakdown and can treat acute bleeding due to elevated fibrinolysis. An orphan drug FDA-approved to prevent recurring hemorrhage in certain patients, aminocaproic acid is also used off-label to control bleeding in patients with immune or nonimmune severe thrombocytopenia (bleeding disorder due to low platelet count). Unlike many other antifibrinolytics, it has no serious side effects at therapeutic doses and there is no evidence that suggests an increased risk of thrombosis.

Aminocaproic acid, brand name Amicar, is a derivate of lysine and is an antifibrinolytic drug. Antifibrinolytics drugs are commonly used during major surgery to prevent significant blood loss. These drugs reversibly blocks the binding sites on plasminogen. This blockade inhibits plasminogen binding to fibrin and the conversion of plasminogen to plasmin. These prevents fibrin degradation and maintains the stability of fibrin clots.

Metabolites of Template4MB1 are predicted with biotransformer.

Amino sugars are sugar molecules containing an amine group. They make up many polysaccharides including, glycosaminoglycans or mucopolysaccharides.

Amino sugars are sugar molecules containing an amine group. They make up many polysaccharides including, glycosaminoglycans or mucopolysaccharides.

Amino sugars are sugar molecules containing an amine group. They make up many polysaccharides including, glycosaminoglycans or mucopolysaccharides.

Amino sugars are sugar molecules containing an amine group. They make up many polysaccharides including, glycosaminoglycans or mucopolysaccharides.

Amino sugars are sugar molecules containing an amine group. They make up many polysaccharides including, glycosaminoglycans or mucopolysaccharides.

The synthesis of amino sugars and nucleotide sugars starts with the phosphorylation of N-Acetylmuramic acid (MurNac) through its transport from the periplasmic space to the cytoplasm. Once in the cytoplasm, MurNac and water undergo a reversible reaction catalyzed by N-acetylmuramic acid 6-phosphate etherase, producing a D-lactic acid and N-Acetyl-D-Glucosamine 6-phosphate. This latter compound can also be introduced into the cytoplasm through a phosphorylating PTS permase in the inner membrane that allows for the transport of N-Acetyl-D-glucosamine from the periplasmic space. N-Acetyl-D-Glucosamine 6-phosphate can also be obtained from chitin dependent reactions. Chitin is hydrated through a bifunctional chitinase to produce chitobiose. This in turn gets hydrated by a beta-hexosaminidase to produce N-acetyl-D-glucosamine. The latter undergoes an atp dependent phosphorylation leading to the production of N-Acetyl-D-Glucosamine 6-phosphate. N-Acetyl-D-Glucosamine 6-phosphate is then be deacetylated in order to produce Glucosamine 6-phosphate through a N-acetylglucosamine-6-phosphate deacetylase. This compound can either be isomerized or deaminated into Beta-D-fructofuranose 6-phosphate through a glucosamine-fructose-6-phosphate aminotransferase and a glucosamine-6-phosphate deaminase respectively. Glucosamine 6-phosphate undergoes a reversible reaction to glucosamine 1 phosphate through a phosphoglucosamine mutase. This compound is then acetylated through a bifunctional protein glmU to produce a N-Acetyl glucosamine 1-phosphate. N-Acetyl glucosamine 1-phosphate enters the nucleotide sugar synthesis by reacting with UTP and hydrogen ion through a bifunctional protein glmU releasing pyrophosphate and a Uridine diphosphate-N-acetylglucosamine.This compound can either be isomerized into a UDP-N-acetyl-D-mannosamine or undergo a reaction with phosphoenolpyruvic acid through UDP-N-acetylglucosamine 1-carboxyvinyltransferase releasing a phosphate and a UDP-N-Acetyl-alpha-D-glucosamine-enolpyruvate. UDP-N-acetyl-D-mannosamine undergoes a NAD dependent dehydrogenation through a UDP-N-acetyl-D-mannosamine dehydrogenase, releasing NADH, a hydrogen ion and a UDP-N-Acetyl-alpha-D-mannosaminuronate, This compound is then used in the production of enterobacterial common antigens. UDP-N-Acetyl-alpha-D-glucosamine-enolpyruvate is reduced through a NADPH dependent UDP-N-acetylenolpyruvoylglucosamine reductase, releasing a NADP and a UDP-N-acetyl-alpha-D-muramate. This compound is involved in the D-glutamine and D-glutamate metabolism.