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Literature summary for 2.1.3.6 extracted from

  • Srivenugopal, K.S.; Adiga, P.R.
    Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase) (1981), J. Biol. Chem., 256, 9532-9541.
    View publication on PubMed
Search for more literature for 2.1.3.6

General Stability

General Stability Organism
highly unstable even in the presence of glycerol, dithiothreitol and Mg2+, activity is stabilized in dilute solutions, less than 0.05 mg protein/ml for about 3-4 h at 37°C by 0.25 mg/ml bovine serum albumine Lathyrus sativus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 1 * 55000, SDS-PAGE Lathyrus sativus
56000
-
 gel filtration Lathyrus sativus

Organism

Organism UniProt Comment Textmining
Lathyrus sativus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
MnCl2, ammonium sulfate, putrescine-CH-Sepharose affinity column Lathyrus 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 Lathyrus sativus
a

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
 Lathyrus sativus
-

Storage Stability

Storage Stability Organism
4°C, 48 h, complete loss of activity Lathyrus sativus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arsenate + N-carbamoylputrescine
-
 Lathyrus sativus ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 55000, SDS-PAGE Lathyrus sativus