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
Agrobacterium tumefaciens C58 / ATCC 33970
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
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
L-aspartate 4-semialdehyde + putrescine + NADPH + H+
carboxyspermidine + H2O + NADP+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+
carboxynorspermidine + H2O + NADP+
show the reaction diagram
L-aspartate 4-semialdehyde + putrescine + NADPH + H+
carboxyspermidine + H2O + NADP+
show the reaction diagram
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
45100
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2 * 45100, SDS-PAGE
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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gene Atu4170, DNA and amino acid sequence determination and analysis of wild-type enzyme mutant genes and enzymes, respectively
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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%
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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transposon mutagenesis of Agrobacterium tumefaciens strain C58 to knockdown enzyme CASDH performed with the mariner minitransposon Himar1, phenotype, overview. In-frame CASDH and CASDC gene deletion mutants have severe growth defects in minimal medium but are rescued in this respect by exogenous addition of exogenous polyamines that supply the 1,3-diaminopropane group, including spermidine. The severe growth defect of the CASDH and CASDC mutants also manifested itself as a severe biofilm deficiency
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