2.5.1.44	2 putrescine	-	Acinetobacter tartarogenes	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	-	Agrobacterium fabrum	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	the enzyme is involved in polyamine biosynthesis pathway	Agrobacterium fabrum	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	-	Agrobacterium fabrum C58	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	the enzyme is involved in polyamine biosynthesis pathway	Agrobacterium fabrum C58	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	-	Agrobacterium tumefaciens	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	spermidine + putrescine	-	Agrobacterium tumefaciens	sym-homospermidine + propane-1,3-diamine	-	?	375303	
2.5.1.44	2 putrescine	-	Blastochloris viridis	sym-homospermidine + NH3	-	?	189565	
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	-	?	189565	
2.5.1.44	2 spermidine	-	Blastochloris viridis	sym-homospermidine + propane-1,3-diamine + putrescine	-	?	436728	
2.5.1.44	additional information	the enzyme has two distinct substrate binding sites, one of which is highly specific for putrescine. Enzyme HSS features a side pocket in the direct vicinity of the active site formed by conserved amino acids and a potential substrate discrimination, guiding, and sensing mechanism. The enzyme is capable of catalyzing side reactions to produce a variety of N-aminobutyl-linked triamines utilizing putrescine together with respective linear diamines with C3 to C7 carbon chains, overview. Bacterial HSS does not produce sym-norspermidine from two 1,4-diaminopropanes	Blastochloris viridis	?	-	?	89	
2.5.1.44	putrescine	-	Blastochloris viridis	sym-homospermidine + NH3 + H+	-	?	436559	
2.5.1.44	putrescine + 1,3-diaminopropane	-	Blastochloris viridis	homospermidine + spermidine	-	?	189567	
2.5.1.44	putrescine + 1,3-diaminopropane	-	Blastochloris viridis	homospermidine + spermidine	low but significant amounts of homologous polyamines in addition to homospermidine	?	189567	
2.5.1.44	putrescine + 1,6 diaminohexane	-	Blastochloris viridis	homospermidine + N-(4-aminobutyl)-1,6-diaminohexane	-	?	189569	
2.5.1.44	putrescine + 1,6 diaminohexane	-	Blastochloris viridis	homospermidine + N-(4-aminobutyl)-1,6-diaminohexane	low but significant amounts of homologous polyamines in addition to homospermidine	?	189569	
2.5.1.44	putrescine + 1,7-diaminoheptane	-	Blastochloris viridis	homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane	-	?	189570	
2.5.1.44	putrescine + 1,7-diaminoheptane	-	Blastochloris viridis	homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane	low but significant amounts of homologous polyamines in addition to homospermidine	?	189570	
2.5.1.44	putrescine + cadaverine	-	Blastochloris viridis	homospermidine + N-(4-aminobutyl)-1,5-diaminopentane	-	?	189568	
2.5.1.44	putrescine + cadaverine	-	Blastochloris viridis	homospermidine + N-(4-aminobutyl)-1,5-diaminopentane	low but significant amounts of homologous polyamines in addition to homospermidine	?	189568	
2.5.1.44	putrescine + spermidine	-	Blastochloris viridis	sym-homospermidine + propane-1,3-diamine	-	?	436558	
2.5.1.44	spermidine	-	Blastochloris viridis	homospermidine + putrescine + 1,3-diaminopropane	-	?	189566	
2.5.1.44	spermidine + 1,6-diaminohexane	-	Blastochloris viridis	homospermidine + N-(4-aminobutyl)-1,6-diaminohexane	-	?	189573	
2.5.1.44	spermidine + cadaverine	-	Blastochloris viridis	homospermidine + N-(4-aminobutyl)-1,5-diaminopentane	-	?	189572	
2.5.1.44	spermidine + cadaverine	-	Blastochloris viridis	(4-aminobutyl)(5-aminopentyl)amine + sym-homospermidine + propane-1,3-diamine + putrescine	-	?	437907	
2.5.1.44	spermidine + putrescine	-	Blastochloris viridis	homospermidine + 1,3-diaminopropane	-	?	189571	
2.5.1.44	spermidine + putrescine	-	Blastochloris viridis	sym-homospermidine + propane-1,3-diamine + putrescine	-	?	437908	
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	-	?	189565	
2.5.1.44	2 putrescine	-	Bradyrhizobium japonicum	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	as partially purified enzymes have been used in the assay the dependence on spermidine for the homospermidine synthesis may have been overlooked. If these enzymes should proof to be spermidine-dependent like other enzymes from plant sources, they must be classified as EC 2.5.1.45	Lathyrus sativus	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	-	Opitutus terrae	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	-	Paramecium tetraurelia	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	-	Ralstonia phage phiRSL1	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	2 putrescine	-	Rhizobium leguminosarum	sym-homospermidine + NH3	-	?	189565	
2.5.1.44	additional information	despite the synthesis of homospermidine, the enzyme also produces 4-aminobutilcadaverine	Rhizobium tropici	?	-	?	89	
2.5.1.44	putrescine	-	Rhizobium tropici	sym-homospermidine + NH3 + H+	-	?	436559	
2.5.1.44	putrescine + spermidine	-	Rhizobium tropici	sym-homospermidine + propane-1,3-diamine	-	?	436558	
2.5.1.44	additional information	despite the synthesis of homospermidine, the enzyme also produces 4-aminobutilcadaverine	Rhizobium tropici Rt CIAT899	?	-	?	89	
2.5.1.44	putrescine	-	Rhizobium tropici Rt CIAT899	sym-homospermidine + NH3 + H+	-	?	436559	
2.5.1.44	putrescine + spermidine	-	Rhizobium tropici Rt CIAT899	sym-homospermidine + propane-1,3-diamine	-	?	436558	
2.5.1.44	2 putrescine	as partially purified enzymes have been used in the assay the dependence on spermidine for the homospermidine synthesis may have been overlooked. If these enzymes should proof to be spermidine-dependent like other enzymes from plant sources, they must be classified as EC 2.5.1.45	Santalum album	sym-homospermidine + NH3	-	?	189565