|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
In Pathway: spermidine biosynthesis I
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: spermidine synthase
Enzyme Commission Synonyms: aminopropyltransferase, putrescine aminopropyltransferase, spermidine synθse, SpeE, S-adenosylmethioninamine:putrescine 3-aminopropyltransferase
This is the fifth and last step in the biosynthesis of spermidine from arginine. It transfers propylamine moiety from S-adenosylmethioninamine to putrescine to form spermidine.
Enzyme Commission Summary:
The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [Pegg81, Yoon00]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [Bowman73, Korolev02]. cf. EC 220.127.116.11, spermine synthase and EC 18.104.22.168, sym-norspermidine synthase.
Korolev02: Korolev S, Ikeguchi Y, Skarina T, Beasley S, Arrowsmith C, Edwards A, Joachimiak A, Pegg AE, Savchenko A (2002). "The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor." Nat Struct Biol 9(1);27-31. PMID: 11731804
Yoon00: Yoon SO, Lee YS, Lee SH, Cho YD (2000). "Polyamine synthesis in plants: isolation and characterization of spermidine synthase from soybean (Glycine max) axes." Biochim Biophys Acta 1475(1);17-26. PMID: 10806333
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