Browsing Pathways

Fatty acid oxidation is also known as beta-oxidation. Fatty acids are an important energy source because they are anhydrous and can be reduced. Fatty acids are good sources of energy as they yield more energy than carbohydrates. The fatty acid oxidation pathway degrades fatty acids into acetyl-CoA under anaerobic and aerobic conditions. Enzymes of this pathway can process short and long chain fatty acids. The first step in the pathway is the conversion of acyl-CoA to enoyl-CoA. The pathway continues in a cycle, each turn removing two carbon atoms from the input acyl-CoA to produce acetyl-CoA. Each turn also produces NADH.

L-alanine is an essential component of proteins and peptidoglycan. The latter also contains about three molecules of D-alanine for every L-alanine. Only about 10 percent of the total alanine synthesized flows into peptidoglycan.There are at least 3 ways to begin the biosynthesis of alanine. The first method for alanine biosynthesis begins with L-cysteine produced from L-cysteine biosynthesis pathway. L-cysteine reacts with an [L-cysteine desulfurase] L-cysteine persulfide through a cysteine desulfurase resulting in a release of [L-cysteine desulfurase] l-cysteine persulfide and L-alanine. The second method starts with pyruvic acid reacting with L-glutamic acid through a glutamate-pyruvate aminotransferase resulting in a oxoglutaric acid and L-alanine. The third method starts with L-glutamic acid interacting with Alpha-ketoisovaleric acid through a valine transaminase resulting in an oxoglutaric acid and L-valine. L-valine reacts with pyruvic acid through a valine-pyruvate aminotransferase resulting Alpha-ketoisovaleric acid and L-alanine. This first step of the pathway, which can be catalyzed by either of two racemases (biosynthetic or catabolic), also serves an essential role in biosynthesis because its product, D-alanine, is an essential component of cell wall peptidoglycan (murein). D-alanine is metabolized by an ATP driven D-alanine ligase A and B resulting in D-alanyl-D-alanine. This product is incorporated into the peptidoglycan biosynthesis. L-alanine is metabolized with alanine racemase, either catabolic or metabolic resulting in a D-alanine. This compound reacts with water and a quinone through a D-amino acid dehydrogenase resulting in Pyruvic acid, hydroquinone and ammonium, thus entering the central metabolism and thereby can serve as a total source of carbon and energy. The role of the dadX racemase is degradative and dadX racemase can be induced by alanine and is subject to catabolite repression.

N-decanoyl-L-homoserine lactone (C10-HSL) is a quorum sensing signaling molecule produced by certain Gram-negative bacteria, such as Pseudomonas species, that enables the coordination of group behaviors like biofilm formation, virulence factor production, and motility. The biosynthesis of C10-HSL is catalyzed by acyl-homoserine lactone (AHL) synthase enzymes, typically homologs of LuxI. The biosynthetic pathway begins with L-homoserine, which serves as the core backbone of the molecule. The C10 fatty acyl group, derived from decanoyl-CoA, is transferred by the AHL synthase enzyme, forming an amide bond with the amino group of L-homoserine. This intermediate is then cyclized to form the lactone ring, resulting in the production of N-decanoyl-L-homoserine lactone (C10-HSL). Additionally, some LuxI homologs can modify the acyl group to include a keto group at the third carbon, resulting in the production of N-(3-oxododecanoyl)-L-homoserine lactone (3-oxo-C10-HSL), which further modulates the quorum sensing response. Both C10-HSL and 3-oxo-C10-HSL act as quorum sensing molecules, diffusing into the extracellular space where their concentration builds as the bacterial population grows. When the concentration of these molecules reaches a critical threshold, they bind to LuxR-type receptors, forming complexes that activate the transcription of genes involved in quorum sensing-regulated behaviors. This system allows bacteria to synchronize their actions in response to population density, enhancing their ability to form biofilms, regulate virulence, and adapt to changing environmental conditions.

Trehalose is a disaccharide made of two glucose molecules that can be used as a store of energy, as well as water retention and protection from freezing at low temperatures. In this pathway, glucose-6-phosphate from the galactose metabolism pathway combines with uridine diphosphate glucose to form alpha,alpha-trehalose 6-phosphate, as well as uridine 5’-diphosphate and a hydrogen ion as byroducts in a reaction catalyzed by alpha,alpha-trehalose-phosphate synthase [UDP-forming]. Following this, alpha,alpha-trehalose 6-phosphate is converted to alpha,alpha-trehalose following the hydrolytic cleavage of its phosphate group by trehalose-phosphate phosphatase. Alpha,alpha-trehalose can then function as energy stores until it is broken down as a part of the trehalose degradation pathway when needed.

Fatty acid oxidation is also known as beta-oxidation. Fatty acids are an important energy source because they are anhydrous and can be reduced. Fatty acids are good sources of energy as they yield more energy than carbohydrates. The fatty acid oxidation pathway degrades fatty acids into acetyl-CoA under anaerobic and aerobic conditions. Enzymes of this pathway can process short and long chain fatty acids. The first step in the pathway is the conversion of acyl-CoA to enoyl-CoA. The pathway continues in a cycle, each turn removing two carbon atoms from the input acyl-CoA to produce acetyl-CoA. Each turn also produces NADH.

Spermidine is formed from decarboxy-SAM and putrescine by catalyzing spermidine synthase (also knowns as polyamine aminopropyltransferase). The source of putrescine is transported from outside of cell by putrescine/spermidine ABC transporter. Decarboxy-SAM comes from S-Adenosylmethionine with catalyzation of adenosylmethionine decarboxylase and cofactors: pyruvic acid and magnesium. The other product of the aminopropyltransferase reaction is S-methyl-5'-thioadenosine (MTA), which can be recycled back to L-methionine in many organisms, but not in E. coli. Inhibition of E. coli adenosylmethionine decarboxylase by spermidine appears to be the most significant regulator of polyamine biosynthesis, probably limiting it when the intracellular spermidine concentration becomes excessive. In E. coli most intracellular spermidine is bound to nucleic acids and phospholipids. (EcoCyc)

Trehalose is a disaccharide made of two glucose molecules that can be used as a store of energy, as well as water retention and protection from freezing at low temperatures. In this pathway, glucose-6-phosphate from the galactose metabolism pathway combines with uridine diphosphate glucose to form alpha,alpha-trehalose 6-phosphate, as well as uridine 5’-diphosphate and a hydrogen ion as byroducts in a reaction catalyzed by alpha,alpha-trehalose-phosphate synthase [UDP-forming]. Following this, alpha,alpha-trehalose 6-phosphate is converted to alpha,alpha-trehalose following the hydrolytic cleavage of its phosphate group by trehalose-phosphate phosphatase. Alpha,alpha-trehalose can then function as energy stores until it is broken down as a part of the trehalose degradation pathway when needed.

The ketogluconate metabolism starts with the degradation of 2,5-didehydro-D-gluconate either through a NADPH dependent 2,5-diketo-D-gluconate reductase resulting in the release of a NADP and 5-dehydro-D-gluconate or through a NADPH dependent 2,5-diketo-D-gluconate reductase protein complex resulting in the release of a NADP and a 2-keto-L-gulonate. The 2-keto-L-gulonate interacts with a NADPH 2-keto-L-gulonate reductase resulting in a NADP and a L-idonate. The L-idonate interacts with a NADP L-idonate 5-dehydrogenase resulting in the release of hydrogen ion, a NADPH and a 5-dehydro-D-gluconate. The 5-dehydro-D-gluconate interacts with a NADPH driven 5-keto-D-gluconate 5-reductase resulting in the release of a NADP and a D-gluconate. The other way to produce D-gluconate is by having 2,5-Didehydro-D-gluconate interacting with a NADPH and hydrogen ion resulting in the release of a NADP and a 2-keto-D-gluconate which then interact with NADPH a 2-keto-D-gluconate reductase resulting in a NADP and a D-gluconate The D-gluconate is phosphorylated by an ATP driven D-gluconate kinase resulting in a ADP, a hydrogen ion and a D-gluconate 6-phosphate. This compound can either join the Entner-Doudoroff pathway or be metabolized by a NADP dependent 6-phosphogluconate dehydrogenase resulting in a NADPH, a carbon dioxide and a D-ribulose 5-phosphate. The Entner-doudoroff pathway is dehydrated by a phosphogluconate dehydratase resulting in a water molecule and a 2-dehydro-3-deoxy-D-gluconate 6-phosphate. This compound then interacts with a 2-keto-3-deoxygluconate 6-phosphate aldolase resulting in a D-glyceraldehyde 3-phosphate and a pyruvic acid. The d-glyceraldehyde 3-phosphate is incorporated into a glycolysis while the pyruvic acid is decarboxylated into acetyl CoA

The ketogluconate metabolism starts with the degradation of 2,5-didehydro-D-gluconate either through a NADPH dependent 2,5-diketo-D-gluconate reductase resulting in the release of a NADP and 5-dehydro-D-gluconate or through a NADPH dependent 2,5-diketo-D-gluconate reductase protein complex resulting in the release of a NADP and a 2-keto-L-gulonate. The 2-keto-L-gulonate interacts with a NADPH 2-keto-L-gulonate reductase resulting in a NADP and a L-idonate. The L-idonate interacts with a NADP L-idonate 5-dehydrogenase resulting in the release of hydrogen ion, a NADPH and a 5-dehydro-D-gluconate. The 5-dehydro-D-gluconate interacts with a NADPH driven 5-keto-D-gluconate 5-reductase resulting in the release of a NADP and a D-gluconate. The other way to produce D-gluconate is by having 2,5-Didehydro-D-gluconate interacting with a NADPH and hydrogen ion resulting in the release of a NADP and a 2-keto-D-gluconate which then interact with NADPH a 2-keto-D-gluconate reductase resulting in a NADP and a D-gluconate The D-gluconate is phosphorylated by an ATP driven D-gluconate kinase resulting in a ADP, a hydrogen ion and a D-gluconate 6-phosphate. This compound can either join the Entner-Doudoroff pathway or be metabolized by a NADP dependent 6-phosphogluconate dehydrogenase resulting in a NADPH, a carbon dioxide and a D-ribulose 5-phosphate. The Entner-doudoroff pathway is dehydrated by a phosphogluconate dehydratase resulting in a water molecule and a 2-dehydro-3-deoxy-D-gluconate 6-phosphate. This compound then interacts with a 2-keto-3-deoxygluconate 6-phosphate aldolase resulting in a D-glyceraldehyde 3-phosphate and a pyruvic acid. The d-glyceraldehyde 3-phosphate is incorporated into a glycolysis while the pyruvic acid is decarboxylated into acetyl CoA

The biosynthesis of Valine and L-leucine from pyruvic acid starts with pyruvic acid interacting with a hydrogen ion through a acetolactate synthase / acetohydroxybutanoate synthase resulting in a release of a carbon dioxide, a (S)-2-acetolactate. The latter compound then interacts with a hydrogen ion through a NADPH-driven acetohydroxy acid isomeroreductase resulting in the release of a NADP, a (R) 2,3-dihydroxy-3-methylvalerate. The latter compound is then dehydrated by a dihydroxy acid dehydratase resulting in the release of a water molecule an 3-methyl-2-oxovaleric acid. The 3-methyl-2-oxovaleric acid can produce an L-valine by interacting with a L-glutamic acid through a Valine Transaminase resulting in the release of a Oxoglutaric acid and a L-valine. The 3-methyl-2-oxovaleric acid then interacts with an acetyl-CoA and a water molecule through a 2-isopropylmalate synthase resulting in the release of a hydrogen ion, a Coenzyme A and a 2-Isopropylmalic acid. The isopropylimalic acid is then hydrated by interacting with a isopropylmalate isomerase resulting in a 3-isopropylmalate. This compound then interacts with an NAD driven 3-isopropylmalate dehydrogenase resulting in a NADH, a hydrogen ion and a 2-isopropyl-3-oxosuccinate. The latter compound then interacts with hydrogen ion spontaneously resulting in a carbon dioxide and a ketoleucine. The ketoleucine then interacts with a L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in the oxoglutaric acid and L-leucine.