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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Reaction: 2.5.1.16

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.5.1.16

Enzymes and Genes:
spermidine synthase Inferred from experiment : speE

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

Summary:
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 2.5.1.22, spermine synthase and EC 2.5.1.23, sym-norspermidine synthase.

Citations: [Hannonen72, Tabor72]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.5.1.16 , ENZYME:EC:2.5.1.16 , IUBMB-ExplorEnz:EC:2.5.1.16


References

Bowman73: Bowman WH, Tabor CW, Tabor H (1973). "Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli." J Biol Chem 1973;248(7);2480-6. PMID: 4572733

Hannonen72: Hannonen P, Janne J, Raina A (1972). "Partial purification and characterization of spermine synthase from rat brain." Biochim Biophys Acta 289(1);225-31. PMID: 4564056

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

Pegg81: Pegg AE, Shuttleworth K, Hibasami H (1981). "Specificity of mammalian spermidine synthase and spermine synthase." Biochem J 197(2);315-20. PMID: 6798961

Tabor72: Tabor H, Tabor CW (1972). "Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines." Adv Enzymol Relat Areas Mol Biol 36;203-68. PMID: 4628436

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc13.