
PathWhiz ID | Pathway | Meta Data |
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PW348579 |
D-Arabinose Degradation IBacteroides finegoldii DSM 17565
Wild-Type E.coli K-12 can not directly use D-arabinose as a sole source of carbon and energy; hence, E.coli uses the enzymes of the fucose degradation pathway to degrade D-arabinose for further utilization. D-arabinose can be metabolized to form dihydroxy-acetone phosphate for entering the central metabolism. Glycolaldehyde can be further catalyzed to form glycolic acid by lactaldehyde dehydrogenase.
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Creator: Julia Wakoli Created On: November 05, 2024 at 18:59 Last Updated: November 05, 2024 at 18:59 |
PW348663 |
D-Arabinose Degradation IParaprevotella clara YIT 11840
Wild-Type E.coli K-12 can not directly use D-arabinose as a sole source of carbon and energy; hence, E.coli uses the enzymes of the fucose degradation pathway to degrade D-arabinose for further utilization. D-arabinose can be metabolized to form dihydroxy-acetone phosphate for entering the central metabolism. Glycolaldehyde can be further catalyzed to form glycolic acid by lactaldehyde dehydrogenase.
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Creator: Julia Wakoli Created On: November 05, 2024 at 20:19 Last Updated: November 05, 2024 at 20:19 |
PW359634 |
D-Arabinose Degradation IEscherichia coli O157:H7 str. Sakai
Wild-Type E.coli K-12 can not directly use D-arabinose as a sole source of carbon and energy; hence, E.coli uses the enzymes of the fucose degradation pathway to degrade D-arabinose for further utilization. D-arabinose can be metabolized to form dihydroxy-acetone phosphate for entering the central metabolism. Glycolaldehyde can be further catalyzed to form glycolic acid by lactaldehyde dehydrogenase.
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Creator: Julia Wakoli Created On: November 14, 2024 at 08:24 Last Updated: November 14, 2024 at 08:24 |
PW359639 |
D-Arabinose Degradation IEscherichia coli HS
Wild-Type E.coli K-12 can not directly use D-arabinose as a sole source of carbon and energy; hence, E.coli uses the enzymes of the fucose degradation pathway to degrade D-arabinose for further utilization. D-arabinose can be metabolized to form dihydroxy-acetone phosphate for entering the central metabolism. Glycolaldehyde can be further catalyzed to form glycolic acid by lactaldehyde dehydrogenase.
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Creator: Julia Wakoli Created On: November 14, 2024 at 08:27 Last Updated: November 14, 2024 at 08:27 |
PW359641 |
D-Arabinose Degradation IEscherichia coli O157:H7 str. EC4115
Wild-Type E.coli K-12 can not directly use D-arabinose as a sole source of carbon and energy; hence, E.coli uses the enzymes of the fucose degradation pathway to degrade D-arabinose for further utilization. D-arabinose can be metabolized to form dihydroxy-acetone phosphate for entering the central metabolism. Glycolaldehyde can be further catalyzed to form glycolic acid by lactaldehyde dehydrogenase.
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Creator: Julia Wakoli Created On: November 14, 2024 at 08:28 Last Updated: November 14, 2024 at 08:28 |
PW359653 |
D-Arabinose Degradation IEscherichia coli O157:H7 str. TW14359
Wild-Type E.coli K-12 can not directly use D-arabinose as a sole source of carbon and energy; hence, E.coli uses the enzymes of the fucose degradation pathway to degrade D-arabinose for further utilization. D-arabinose can be metabolized to form dihydroxy-acetone phosphate for entering the central metabolism. Glycolaldehyde can be further catalyzed to form glycolic acid by lactaldehyde dehydrogenase.
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Creator: Julia Wakoli Created On: November 14, 2024 at 08:33 Last Updated: November 14, 2024 at 08:33 |
PW088310 |
D-Arginine and D-Ornithine MetabolismRattus norvegicus
D-Amino acids have been show to be present in high concentrations in humans and play a role in biological functions. D-Amino may have negative effects as they can be found in some bacteria or form spontaneously in certain reactions. D-Amino acid oxidase (DAAO) is one of the main enzymes that metabolize D-Amino acids via deamination. DAAO is highly specific towards D-amino acids and favours free neutral D-amino acids or those with hydrophobic, polar or aromatic groups. Acidic amino acids are not catalyze by DAOO.
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Creator: Ana Marcu Created On: August 10, 2018 at 13:36 Last Updated: August 10, 2018 at 13:36 |
PW088397 |
D-Arginine and D-Ornithine MetabolismDrosophila melanogaster
D-Amino acids have been show to be present in high concentrations in humans and play a role in biological functions. D-Amino may have negative effects as they can be found in some bacteria or form spontaneously in certain reactions. D-Amino acid oxidase (DAAO) is one of the main enzymes that metabolize D-Amino acids via deamination. DAAO is highly specific towards D-amino acids and favours free neutral D-amino acids or those with hydrophobic, polar or aromatic groups. Acidic amino acids are not catalyze by DAOO.
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Creator: Ana Marcu Created On: August 10, 2018 at 15:44 Last Updated: August 10, 2018 at 15:44 |
PW000019 |
D-Arginine and D-Ornithine MetabolismHomo sapiens
D-Amino acids have been show to be present in high concentrations in humans and play a role in biological functions. D-Amino may have negative effects as they can be found in some bacteria or form spontaneously in certain reactions. D-Amino acid oxidase (DAAO) is one of the main enzymes that metabolize D-Amino acids via deamination. DAAO is highly specific towards D-amino acids and favours free neutral D-amino acids or those with hydrophobic, polar or aromatic groups. Acidic amino acids are not catalyze by DAOO.
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Creator: WishartLab Created On: August 01, 2013 at 13:54 Last Updated: August 01, 2013 at 13:54 |
PW088209 |
D-Arginine and D-Ornithine MetabolismBos taurus
D-Amino acids have been show to be present in high concentrations in humans and play a role in biological functions. D-Amino may have negative effects as they can be found in some bacteria or form spontaneously in certain reactions. D-Amino acid oxidase (DAAO) is one of the main enzymes that metabolize D-Amino acids via deamination. DAAO is highly specific towards D-amino acids and favours free neutral D-amino acids or those with hydrophobic, polar or aromatic groups. Acidic amino acids are not catalyze by DAOO.
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Creator: Ana Marcu Created On: August 10, 2018 at 11:11 Last Updated: August 10, 2018 at 11:11 |