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Literature summary for 2.1.3.6 extracted from

  • Prasad, G.L.; Adiga, P.R.
    Purification and characterization of putrescine synthase from cucumber seedlings. A multifunctional enzyme involved in putrescine biosynthesis (1986), J. Biosci., 10, 373-391.
No PubMed abstract available

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15000
-
x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol Cucumis sativus
18000
-
x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol Cucumis sativus
44000
-
x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol Cucumis sativus
150000
-
x * 150000, SDS-PAGE, nonreducing Cucumis sativus

Organism

Organism UniProt Comment Textmining
Cucumis sativus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine multifunctional enzyme that catalyzes the reactions of EC 2.1.3.3 ornithine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively Cucumis sativus

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
Cucumis sativus
-

Subunits

Subunits Comment Organism
? x * 150000, SDS-PAGE, nonreducing Cucumis sativus
? x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol Cucumis sativus