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Information on EC 2.5.1.23 - sym-norspermidine synthase and Organism(s) Hyperthermus butylicus and UniProt Accession A2BJU2

for references in articles please use BRENDA:EC2.5.1.23
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EC Tree
IUBMB Comments
The enzyme has been originally characterized from the protist Euglena gracilis [1,2]. The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylsulfanyl)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency . cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.22 (spermine synthase).
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This record set is specific for:
Hyperthermus butylicus
UNIPROT: A2BJU2
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The taxonomic range for the selected organisms is: Hyperthermus butylicus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Synonyms
HbSpe 1, propylaminc transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminopropyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl 3-(methylthio)propylamine:propane-1,3-diamine 3-aminopropyltransferase
The enzyme has been originally characterized from the protist Euglena gracilis [1,2]. The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylsulfanyl)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency [3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.22 (spermine synthase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine
S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine
show the reaction diagram
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + thermospermine + H+
show the reaction diagram
at 5% of the specific activity compared to propane-1,3-diamine
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
pH 7.5, 95°C, substrate: spermidine
0.038
pH 7.5, 95°C, substrate: propane-1,3-diamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34437
x * 34437, calculation from sequence
37000
x * 37000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli with an N-terminal 6* His sequence
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Knott, J.M.
Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum
FEBS Lett.
583
3519-3524
2009
Hyperthermus butylicus (A2BJU2), Hyperthermus butylicus DSM 5456 (A2BJU2)
Manually annotated by BRENDA team