EC Number   |
Reaction |
Reference |
|---|
   2.5.1.44 | putrescine + spermidine = sym-homospermidine + propane-1,3-diamine |
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| 2.5.1.44 | 2 putrescine = sym-homospermidine + NH3 + H+ |
the reaction mechanism emphasizes cation-Pi interaction through a conserved Trp residue as a key stabilizer of high energetic transition states. 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 |
739672 |
| 2.5.1.44 | putrescine + spermidine = sym-homospermidine + propane-1,3-diamine |
the reaction mechanism emphasizes cation-Pi interaction through a conserved Trp residue as a key stabilizer of high energetic transition states. 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 |
739672 |
| 2.5.1.44 | 2 putrescine = sym-homospermidine + NH3 + H+ |
the reaction of this enzyme occurs in three steps: i. NAD-dependent dehydrogenation of putrescine, ii. transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine, iii. reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. In the presence of putrescine, spermidine can function as a donor of the aminobutyl group, in which case, propane-1,3-diamine is released instead of ammonia. Differs from EC 2.5.1.45, homospermidine synthase, spermidine-specific, which cannot use putrescine as donor of the aminobutyl group |
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