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PW492167

Pw492167 View Pathway
metabolic

Spermidine Biosynthesis I

Campylobacter upsaliensis JV21
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: February 01, 2025 at 02:50

Last Updated: February 01, 2025 at 02:50

PW492174

Pw492174 View Pathway
metabolic

Spermidine Biosynthesis I

Campylobacter showae CSUNSWCD
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: February 01, 2025 at 02:53

Last Updated: February 01, 2025 at 02:53

PW490849

Pw490849 View Pathway
metabolic

Spermidine Biosynthesis I

Bacteroides xylanisolvens SD CC 1b
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: January 31, 2025 at 15:05

Last Updated: January 31, 2025 at 15:05

PW492011

Pw492011 View Pathway
metabolic

Spermidine Biosynthesis I

Neisseria cinerea ATCC 14685
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: February 01, 2025 at 01:19

Last Updated: February 01, 2025 at 01:19

PW492655

Pw492655 View Pathway
metabolic

Spermidine Biosynthesis I

Haemophilus haemolyticus M19501
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: February 01, 2025 at 07:42

Last Updated: February 01, 2025 at 07:42

PW488899

Pw488899 View Pathway
metabolic

Spermidine Biosynthesis I

Alistipes shahii WAL 8301
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: January 30, 2025 at 21:10

Last Updated: January 30, 2025 at 21:10

PW491140

Pw491140 View Pathway
metabolic

Spermidine Biosynthesis I

Porphyromonas uenonis 60-3
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: January 31, 2025 at 17:34

Last Updated: January 31, 2025 at 17:34

PW491138

Pw491138 View Pathway
metabolic

Spermidine Biosynthesis I

Alloprevotella tannerae ATCC 51259
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: January 31, 2025 at 17:34

Last Updated: January 31, 2025 at 17:34

PW491974

Pw491974 View Pathway
metabolic

Spermidine Biosynthesis I

Eikenella corrodens ATCC 23834
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: February 01, 2025 at 00:55

Last Updated: February 01, 2025 at 00:55

PW490743

Pw490743 View Pathway
metabolic

Spermidine Biosynthesis I

Bacteroides nordii CL02T12C05
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)
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: January 31, 2025 at 14:15

Last Updated: January 31, 2025 at 14:15