Information on EC 1.5.1.43 - carboxynorspermidine synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.43
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RECOMMENDED NAME
GeneOntology No.
carboxynorspermidine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carboxynorspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+
show the reaction diagram
(1)
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carboxyspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + putrescine + NADPH + H+
show the reaction diagram
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
norspermidine biosynthesis
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spermidine biosynthesis II
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polyamine pathway
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Arginine and proline metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
carboxynorspermidine:NADP+ oxidoreductase
The reaction takes place in the opposite direction. Part of a bacterial polyamine biosynthesis pathway. L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine/carboxyspermidine, respectively [1]. The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation [2]. The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carboxynorspermidine + H2O + NADP+
L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+
show the reaction diagram
carboxyspermidine + H2O + NADP+
L-aspartate 4-semialdehyde + putrescine + NADPH + H+
show the reaction diagram
L-aspartate 4-semialdehyde + propane-1,3-diamine + NADH + H+
carboxynorspermidine + H2O + NAD+
show the reaction diagram
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NADH is a much poorer cofactor than NADPH
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?
L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+
carboxynorspermidine + H2O + NADP+
show the reaction diagram
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?
L-aspartate 4-semialdehyde + putrescine + NADPH + H+
carboxyspermidine + H2O + NADP+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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NADH is a much poorer cofactor than NADPH
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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Ca2+, Mg2+, Fe3+, Fe2+, Cu+, Cu2+, Mn2+, Zn2+, Na+ and K+ at 1 M have no effect on enzyme activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
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24% inhibition at 5 mM
N-ethylmaleimide
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83% inhibition at 5 mM
additional information
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EDTA (1 mM) shows no significant inhibitory effect on enzyme activity; NAD+, ATP and SPD are not inhibitory at 5 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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about 14fold increase of activity at 20 mM. Without addition of dithiothreitol to the assay mixture, only 7% of the maximum activity is detected in the purified enzyme
additional information
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EDTA (1 mM) shows no significant stimulatory effect on enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.97
NADH
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at pH 7.5 and 37C
1.51
NADPH
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at pH 7.5 and 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0167
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crude enzyme, at pH 7.5 and 37C
31
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after 1856fold purification, at pH 7.5 and 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 8
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85% and 18% of the maximum activity are observed at pH 8.0 and 6.3, respectively
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
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78% and 59% of the maximum activity remain at 30C and 45C, respectively, but no activity is observed above 50C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2 - 4.3
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
93500
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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the enzyme is unstable in buffers of pH below 6.5. At pH 6.5, 50% loss of activity is observed within 12 h at 4C
712623
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, in 20 mM Tris/HCl, pH 7.5, containing 1 mM dithiothreitol and 0.02% (v/v) NaN3, 1 week, 15% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Blue Sepharose CL-6B column chromatography, DEAE-Sepharose column chromatography, and hydroxyapatite column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
when Vibrio alginolyticus is grown in the presence of 5 mM norspermidine, the specific activity of the enzyme is reduced by about 70%