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 |
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 |
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 |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.5.1.44 | 73000 | - |
gel filtration | Blastochloris viridis |
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 | - |
? |
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 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.5.1.44 | 200fold | Blastochloris viridis |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.5.1.44 | culture medium | crude extract after ultrasonication and centrifugation | Blastochloris viridis | - |
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 | - |
? |
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 |