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Literature summary for 2.5.1.44 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
Search for more literature for 2.5.1.44

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 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

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

Purification (Commentary)

Purification (Comment) Organism
200fold Blastochloris viridis

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 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

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