Pathway details: β-alanine biosynthesis I
General info
Interaction details
Linked pathways
Protein-protein interactions
Notes
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Pathway was created on Thu Jun 2, 2011.
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 | | Contributed by aracyc: General Information: β-Alanine is a central component of pantothenate biosynthesis. In bacteria the synthesis of β-alanine occurs through the decarboxylation of L-aspartate. This route of biosynthesis however appears to be unique to prokaryotes and absent in eukaryotes. In several plants species as well as yeast β-alanine was shown to be derived from the degradation of polyamines such as spermine and spermidine. Radiotracer experiments in Zea mays showed that maize shoots can convert spermidine and spermine to β-alanine and its biosynthesis intermediate 1,3-diaminopropane |CITS:[Terano78]|. Similarly fruit pericarp discs of tomato (Lycopersicon esculentum) were shown to catabolize radiolabeled spermidine to putrescine and β-alanine |CITS:[rastogi89]|. Enzymes: Most of the enzymes of this pathway have been purified and characterized, albeit in different organisms. Several plant FAD-containging polyamine oxidases (PAOs) have been isolated of which maize PAO (MPAO) has been the most extensively studied so far and for which a tertiary structure is available. Plant PAOs are predominantly localized in the cell wall where their H2O2-generating activity is thought to play a role in lignin biosynthesis and cell wall cross-linking reactions which may regulate growth and contribute to cell defense . PAOs are generally able to use more than one amine substrates such as spermidine, spermine, cadaverine or putrescine depending on the enzyme considered , . Kinetic information on the other two enzymes of the pathway, namely diamine oxidase and 3-aminopropionaldehyde dehydrogenase, are also available. In AraCyc: It is uncertain whether this pathway exists in Arabidopsis thaliana. It has nonetheless been retained in the database on the basis of its existence in other plant species.
Contributed by aracyc: General Information: β-Alanine is a central component of pantothenate biosynthesis. In bacteria the synthesis of β-alanine occurs through the decarboxylation of L-aspartate. This route of biosynthesis however appears to be unique to prokaryotes and absent in eukaryotes. In several plants species as well as yeast β-alanine was shown to be derived from the degradation of polyamines such as spermine and spermidine. Radiotracer experiments in Zea mays showed that maize shoots can convert spermidine and spermine to β-alanine and its biosynthesis intermediate 1,3-diaminopropane |CITS:[Terano78]|. Similarly fruit pericarp discs of tomato (Lycopersicon esculentum) were shown to catabolize radiolabeled spermidine to putrescine and β-alanine |CITS:[rastogi89]|. Enzymes: Most of the enzymes of this pathway have been purified and characterized, albeit in different organisms. Several plant FAD-containging polyamine oxidases (PAOs) have been isolated of which maize PAO (MPAO) has been the most extensively studied so far and for which a tertiary structure is available. Plant PAOs are predominantly localized in the cell wall where their H2O2-generating activity is thought to play a role in lignin biosynthesis and cell wall cross-linking reactions which may regulate growth and contribute to cell defense . PAOs are generally able to use more than one amine substrates such as spermidine, spermine, cadaverine or putrescine depending on the enzyme considered , . Kinetic information on the other two enzymes of the pathway, namely diamine oxidase and 3-aminopropionaldehyde dehydrogenase, are also available. In AraCyc: It is uncertain whether this pathway exists in Arabidopsis thaliana. It has nonetheless been retained in the database on the basis of its existence in other plant species.
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 | | Parts of this pathway occur in:
nucleus cytosol |
interactions
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 cytosol |
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Participating entities and compounds
Browse entities [39]:
By type
Sources & sinks
All entities
1,3-diaminopropane,
1,5-diazabicyclononane,
1-(3-aminopropyl)-4-aminobutanal,
1-(3-aminopropyl)-pyrrolinium,
1-pyrroline,
3-aminopropionaldehyde,
4-aminobutanal,
a reduced acceptor,
an acceptor,
AT1G62830 / LSD1-like 1,
AT1G62830 / LSD1-like 1,
AT1G62830 / LSD1-like 1,
AT2G43020 / polyamine oxidase 2,
AT2G43020 / polyamine oxidase 2,
AT2G43020 / polyamine oxidase 2,
AT3G10390 / Flavin containing amine oxidoreductase family prot,
AT3G10390 / Flavin containing amine oxidoreductase family prot,
AT3G10390 / Flavin containing amine oxidoreductase family prot,
AT3G13682 / LSD1-like2,
AT3G13682 / LSD1-like2,
AT3G13682 / LSD1-like2,
AT4G16310 / LSD1-like 3,
AT4G16310 / LSD1-like 3,
AT4G16310 / LSD1-like 3,
AT4G29720 / polyamine oxidase 5,
AT4G29720 / polyamine oxidase 5,
AT4G29720 / polyamine oxidase 5,
beta-alanine,
H2O,
H2O2,
H+,
NAD(P)+,
NAD(P)H,
NH3,
O2,
polyamine oxidase-activity-15927,
spermidine,
spermine,
135609,
| Type |
metabolite [19] |
| | 1,3-diaminopropane, 1,5-diazabicyclononane, 1-(3-aminopropyl)-4-aminobutanal, 1-(3-aminopropyl)-pyrrolinium, 1-pyrroline, 3-aminopropionaldehyde, 4-aminobutanal, a reduced acceptor, an acceptor, beta-alanine, H2O, H2O2, H+, NAD(P)+, NAD(P)H, NH3, O2, spermidine, spermine, |
RNA [6] |
| | AT1G62830 / LSD1-like 1, AT2G43020 / polyamine oxidase 2, AT3G10390 / Flavin containing amine oxidoreductase family prot, AT3G13682 / LSD1-like2, AT4G16310 / LSD1-like 3, AT4G29720 / polyamine oxidase 5, |
polypeptide [7] |
| | AT1G62830 / LSD1-like 1, AT2G43020 / polyamine oxidase 2, AT3G10390 / Flavin containing amine oxidoreductase family prot, AT3G13682 / LSD1-like2, AT4G16310 / LSD1-like 3, AT4G29720 / polyamine oxidase 5, 135609, |
gene [6] |
| | AT1G62830 / LSD1-like 1, AT2G43020 / polyamine oxidase 2, AT3G10390 / Flavin containing amine oxidoreductase family prot, AT3G13682 / LSD1-like2, AT4G16310 / LSD1-like 3, AT4G29720 / polyamine oxidase 5, |
protein complex [1] |
| | polyamine oxidase-activity-15927, |