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Information on EC 2.5.1.127 - caldopentamine synthase and Organism(s) Hyperthermus butylicus and UniProt Accession A2BIX4

for references in articles please use BRENDA:EC2.5.1.127
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EC Tree
IUBMB Comments
The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.23, sym-norspermidine synthase and EC 2.5.1.126, norspermine synthase, this enzyme shows no activity with propane-1,3-diamine.
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This record set is specific for:
Hyperthermus butylicus
UNIPROT: A2BIX4
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The taxonomic range for the selected organisms is: Hyperthermus butylicus
The expected taxonomic range for this enzyme is: Hyperthermus butylicus
Synonyms
HbSpe II, long-chain polyamine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
long-chain polyamine synthase
ambiguous
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl 3-(methylthio)propylamine:norspermine 3-aminopropyltransferase
The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.23, sym-norspermidine synthase and EC 2.5.1.126, norspermine synthase, this enzyme shows no activity with propane-1,3-diamine.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl 3-(methylthio)propylamine + caldopentamine
S-methyl-5'-thioadenosine + caldoheptamine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + caldopentamine
S-methyl-5'-thioadenosine + caldohexamine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + norspermidine
S-methyl-5'-thioadenosine + norspermine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + norspermine
S-methyl-5'-thioadenosine + caldopentamine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine
S-methyl-5'-thioadenosine + norspermidine
show the reaction diagram
at 2% of the specific activity compared to norspermine
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + thermospermine + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl 3-(methylthio)propylamine + caldopentamine
S-methyl-5'-thioadenosine + caldoheptamine
show the reaction diagram
the long-chain polyamines stabilize double-stranded DNA at high temperatures
-
-
?
S-adenosyl 3-(methylthio)propylamine + caldopentamine
S-methyl-5'-thioadenosine + caldohexamine
show the reaction diagram
the long-chain polyamines stabilize double-stranded DNA at high temperatures
-
-
?
S-adenosyl 3-(methylthio)propylamine + norspermidine
S-methyl-5'-thioadenosine + norspermine
show the reaction diagram
the long-chain polyamines stabilize double-stranded DNA at high temperatures
-
-
?
S-adenosyl 3-(methylthio)propylamine + norspermine
S-methyl-5'-thioadenosine + caldopentamine
show the reaction diagram
the long-chain polyamines stabilize double-stranded DNA at high temperatures
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + thermospermine + H+
show the reaction diagram
spermidine is not the most preferred substrate for any enzyme. Nevertheless, in vivo the enzyme can be responsible for the synthesis of thermospermine, if spermidine is present in a high concentration in competition to other accepted polyamines
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
pH 7.5, 95°C, substrate: propane-1,3-diamine
0.018
pH 7.5, 95°C, substrate: spermidine
0.064
pH 7.5, 95°C, substrate: norspermidine
0.112
pH 7.5, 95°C, substrate: norspermine
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
32400
x * 32400, calculation from sequence
35000
x * 35000, 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 (A2BIX4), Hyperthermus butylicus DSM 5456 (A2BIX4)
Manually annotated by BRENDA team