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Literature summary extracted from

  • Tait, G.H.
    The formation of homospermidine by an enzyme from Rhodopseudomonas viridis (1979), Biochem. Soc. Trans., 7, 199-200.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.44 1,3-diaminopropane strong competitive inhibitor, Ki: 0.002 mM Blastochloris viridis
2.5.1.44 1,5-Diaminopentane weak inhibition Blastochloris viridis
2.5.1.44 additional information 4-aminobutyraldehyde, postulated intermediate, no inhibition Blastochloris viridis
2.5.1.44 NADH competitive inhibitor, Ki: 0.0015 mM Blastochloris viridis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.44 0.0025
-
 NAD+
-
 Blastochloris viridis
2.5.1.44 0.2
-
 putrescine
-
 Blastochloris viridis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.44 K+ optimal activity with 40 mM, Na+ and Rb+ are less effective Blastochloris viridis
2.5.1.44 Na+ less effective than K+ in activation Blastochloris viridis
2.5.1.44 Rb+ less effective than K+ in activation Blastochloris viridis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.44 73000
-
 gel filtration Blastochloris viridis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.44 2 putrescine Blastochloris viridis one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine sym-homospermidine + NH3
-
 ?
2.5.1.44 2 putrescine Blastochloris viridis N.C.I.B. 10028 one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine sym-homospermidine + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.44 Blastochloris viridis
-
 accession no. L77975
-
2.5.1.44 Blastochloris viridis
-
 N.C.I.B. 10028
-
2.5.1.44 Blastochloris viridis N.C.I.B. 10028
-
 N.C.I.B. 10028
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.44 200fold Blastochloris viridis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.44 culture medium crude extract after ultrasonication and centrifugation Blastochloris viridis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.44 2 putrescine one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine Blastochloris viridis sym-homospermidine + NH3
-
 ?
2.5.1.44 2 putrescine one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine Blastochloris viridis N.C.I.B. 10028 sym-homospermidine + NH3
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.44 NAD+ cannot be replaced by NADP+, NADPH, NADH Blastochloris viridis
2.5.1.44 NAD+ required in catalytic amounts with a Km-value of 0.0025 mM Blastochloris viridis