2.5.1.16: spermidine synthase
This is an abbreviated version!
For detailed information about spermidine synthase, go to the full flat file.
Word Map on EC 2.5.1.16
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2.5.1.16
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polyamine
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spermine
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s-adenosylmethionine
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ornithine
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diamine
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samdc
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dicyclohexylamine
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alpha-difluoromethylornithine
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5'-methylthioadenosine
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cadaverine
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trypanothione
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adometdc
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agmatine
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4.1.1.50
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difluoromethylornithine
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medicine
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drug development
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methylthioadenosine
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thermospermine
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nutrition
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1,3-diaminopropane
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biotechnology
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norspermidine
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multisubstrate
- 2.5.1.16
- polyamine
- spermine
- s-adenosylmethionine
- ornithine
- diamine
- samdc
- dicyclohexylamine
- alpha-difluoromethylornithine
- 5'-methylthioadenosine
- cadaverine
- trypanothione
- adometdc
- agmatine
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4.1.1.50
- difluoromethylornithine
- medicine
- drug development
- methylthioadenosine
- thermospermine
- nutrition
- 1,3-diaminopropane
- biotechnology
- norspermidine
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multisubstrate
Reaction
Synonyms
aminopropyltransferase, aminopropyltransferase spermidine synthase, AtSPDS1, AtSPDS2, MdSPDS1, PAPT, PgSPD, putrescine aminopropyltransferase, Spd synthase, SPDS, SPDS2, SPDSYN, spe-sdh, spe3, SpeE, spermidine synthase, spermidine synthase 1, spermidine synthetase, Spm synthase, SpSyn, Synpcc7942_0628, synthase, spermidine
ECTree
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Reaction
Reaction on EC 2.5.1.16 - spermidine synthase
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
Michaelis-Menten kinetics
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
first discovered
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
uni uni uni uni ping pong mechanism
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
ping-pong mechanism with a propylaminated form of the enzyme as an obligatory intermediate
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
single displacement reaction
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
single displacement reaction
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
single displacement reaction
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
general mechanistic hypothesis for the aminopropyl transfer reaction
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
general mechanistic hypothesis for the aminopropyl transfer reaction
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
reaction mechanism involving a gate-keeping loop, active site and substrate binding structures and involved residues, structure-function relationship analysis by molecular dynamics simulations of a homology model
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
the enzyme possesses a Rossmann-like fold with a distinct active site, the enzyme from Helicobacter pylori lacks the gatekeeping loop that facilitates substrate binding in other PAPTs, active site structure
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
Escherichia coli SPDS follows the ping-pong mechanism, in which an aminopropylated enzyme intermediate was formed by the interaction of SPDS with dcSAM, prior to reaction with putrescine
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
this mechanism depends on a conserved Asp (residue 173 in hSpdS) in the active site that interacts with the bound amine substrate to deprotonate the attacking nitrogen atom of the amine. This interaction is reinforced by additional interactions of this nitrogen atom with the hydroxyl group of a conserved Tyr (residue 79 in hSpdS) and a backbone carbonyl group (Ser174 in hSpdS). These interactions allow the attack on the methylene carbon atom of the aminopropyl group attached to the sulfonium center of dcAdoMet. Electron transfer to this sulfur atom completes the reaction forming S-methyl-5'-thioadenosine and the polyamine product. The positively charged sulfonium ion is a critical part of the reaction
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
random order or ordered mechanism in which both substrates bind before the release of the products
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