Browsing Pathways

L-lyxose is a sugar and a monosaccharide containing five carbon atoms and aldehyde group. Wild-type E.coli can't utilize L-lyxose as its source of carbon and energy. In mutated E.coli, it can metabolize l-lyxose through utilization of enzymes of the rhamnose, arabinose and 2,3-diketo-L-gulonate systems. β-L-lyxopyranose enter cell by L-rhamnose-proton symporter, then convert to l-xylulose by L-rhamnose isomerase. L-xylulose is further metabolized to L-xylulose-5-phosphate with energy ATP. Putative L-ribulose-5-phosphate 3-epimerase can convert L-xylulose -5-phosphate to L-ribulose 5-phosphate, and L-ribulose 5-phosphate 4-epimerase can catalyze L-ribulose 5-phosphate to xylulose 5-phosphate for further pentose phosphate.

Methylglyoxal, also known as pyruvaldehyde, is a cytotoxic compound derived from pyruvic acid. In E. coli, there are at least eight pathways that are responsible for the detoxification of methylglyoxal. The first reaction in this pathway is the reduction of pyruvaldehyde to (S)-lactaldehyde, along with the cofactor NADH, catalyzed by 2,5-diketo-D-gluconic acid reductase subunits A and B. Following this, (S)-lactaldehyde is dehydrogenated into L-lactic acid by the lactaldehyde dehydrogenase enzyme, also using NAD as a cofactor. Finally, L-lactic acid is converted to pyruvic acid by L-lactate dehydrogenase in a reaction involving the reduction of an electron acceptor. Pyruvic acid is then used in glycolysis and pyruvate dehydrogenase pathways.

Methylglyoxal, also known as pyruvaldehyde, is a cytotoxic compound derived from pyruvic acid. In E. coli, there are at least eight pathways that are responsible for the detoxification of methylglyoxal. The first reaction in this pathway is the reversible reduction of pyruvaldehyde to hydroxyacetone, along with the cofactor NADPH, catalyzed by an uncharacterized protein encoded by the yghZ gene, now known to be L-glyceraldehyde 3-phosphate reductase. Following this, hydroxyacetone is oxidized into (S)-propane-1,2-diol by the glycerol dehydrogenase enzyme, using NAD as a cofactor. Finally, (S)-propane-1,2-diol is transported into the periplasmic space.

Methylglyoxal, also known as pyruvaldehyde, is a cytotoxic compound derived from pyruvic acid. In E. coli, there are at least eight pathways that are responsible for the detoxification of methylglyoxal. The first reaction in this pathway is the reversible reduction of pyruvaldehyde to hydroxyacetone, along with the cofactor NADPH, catalyzed by an uncharacterized protein encoded by the yghZ gene, now known to be L-glyceraldehyde 3-phosphate reductase. Following this, hydroxyacetone is oxidized into (S)-propane-1,2-diol by the glycerol dehydrogenase enzyme, using NAD as a cofactor. Finally, (S)-propane-1,2-diol is transported into the periplasmic space.

L-lyxose is a sugar and a monosaccharide containing five carbon atoms and aldehyde group. Wild-type E.coli can't utilize L-lyxose as its source of carbon and energy. In mutated E.coli, it can metabolize l-lyxose through utilization of enzymes of the rhamnose, arabinose and 2,3-diketo-L-gulonate systems. β-L-lyxopyranose enter cell by L-rhamnose-proton symporter, then convert to l-xylulose by L-rhamnose isomerase. L-xylulose is further metabolized to L-xylulose-5-phosphate with energy ATP. Putative L-ribulose-5-phosphate 3-epimerase can convert L-xylulose -5-phosphate to L-ribulose 5-phosphate, and L-ribulose 5-phosphate 4-epimerase can catalyze L-ribulose 5-phosphate to xylulose 5-phosphate for further pentose phosphate.

Methylglyoxal, also known as pyruvaldehyde, is a cytotoxic compound derived from pyruvic acid. In E. coli, there are at least eight pathways that are responsible for the detoxification of methylglyoxal. The first reaction in this pathway is the reduction of pyruvaldehyde to (S)-lactaldehyde, along with the cofactor NADH, catalyzed by 2,5-diketo-D-gluconic acid reductase subunits A and B. Following this, (S)-lactaldehyde is dehydrogenated into L-lactic acid by the lactaldehyde dehydrogenase enzyme, also using NAD as a cofactor. Finally, L-lactic acid is converted to pyruvic acid by L-lactate dehydrogenase in a reaction involving the reduction of an electron acceptor. Pyruvic acid is then used in glycolysis and pyruvate dehydrogenase pathways.

Methylglyoxal, also known as pyruvaldehyde, is a cytotoxic compound derived from pyruvic acid. In E. coli, there are at least eight pathways that are responsible for the detoxification of methylglyoxal. The first reaction in this pathway is the reduction of pyruvaldehyde to (S)-lactaldehyde, along with the cofactor NADH, catalyzed by 2,5-diketo-D-gluconic acid reductase subunits A and B. Following this, (S)-lactaldehyde is dehydrogenated into L-lactic acid by the lactaldehyde dehydrogenase enzyme, also using NAD as a cofactor. Finally, L-lactic acid is converted to pyruvic acid by L-lactate dehydrogenase in a reaction involving the reduction of an electron acceptor. Pyruvic acid is then used in glycolysis and pyruvate dehydrogenase pathways.

The benzoate catabolism pathway is a key metabolic pathway that allows bacteria to utilize benzoate as a carbon source and involves the conversion of benzoate into intermediates that can enter the citric acid cycle. The benABCD operon responsible contains 4 genes benA, benB, benC, benD. The operon is activated by the benM gene which encodes for a transcriptional regulator and is outside of this operon. This operon is activated in the presence of benzoate, which binds to the transcriptional regulator, enhancing its ability to bind the promoter and facilitate RNA polymerase recruitment, thus initiating transcription. benA encodes benzoate 1,2-dioxygenase alpha subunit, which is part of the enzyme complex that catalyzes the initial dioxygenation of benzoate to form catechol which enters the catechil ortho-cleavage pathway and eventually feeds the TCA cycle. benB encodes benzoate 1,2-dioxygenase beta subunit, which works in conjunction with BenA to catalyze the same reaction. benC encodes a reductase that reduces NAD to NADH which is required in the BenAB complex for the dioxygenation reaction to form dihydrodiol. benD encodes cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase, which converts the intermediate product (dihydrodiol) into catechol. Additionally, the operon is influenced by benK and benP which are also outside of the operon and encode for membrane transporters involved in the uptake of benzoate into the cell.

The areCBA operon in Acinetobacter sp. strain ADP1 is activated in response to the presence of aromatic compounds, particularly benzyl acetate, which diffuses into the bacterial cell when its extracellular concentration reaches a threshold level. Upon entry into the cell, benzyl acetate serves as an inducer that triggers the transcriptional activation of the operon through the action of the regulatory protein AreR. AreR, a member of the NtrC/XylR family, binds to specific regulatory sequences located upstream of the promoter region of the areCBA operon, enhancing the RNA polymerase recruitment and initiation of transcription. The operon comprises three genes: areA, areB, and areC. The AreA protein, an esterase, catalyzes the hydrolysis of benzyl acetate, converting it into benzyl alcohol and acetic acid, thereby initiating the degradation process. Subsequently, the alcohol is converted into benzaldehyde by the action of AreB, an alcohol dehydrogenase, which facilitates the oxidation of benzyl alcohol to its corresponding aldehyde. Finally, AreC, a dehydrogenase, further processes benzaldehyde into salicylate, which integrates into the β-ketoadipate pathway for subsequent degradation, allowing the bacteria to utilize these aromatic compounds as carbon sources. This structured sequence of reactions, coupled with AreR's regulatory function, ensures efficient catabolism of benzyl alkanoates, allowing Acinetobacter sp. strain ADP1 to thrive in environments rich in these compounds. The coordinate induction of the areCBA operon through AreR exemplifies a finely tuned mechanism that responds dynamically to environmental cues, ultimately facilitating the bacterium's adaptability and metabolic versatility.