Information on EC 1.4.1.B4 - carboxynorspermidine dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.4.1.B4
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
carboxynorspermidine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+ = carboxynorspermidine + NADP+ + H2O
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
(3-((3-aminopropyl)amino)propyl)carbamate:NADP+ oxidase
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CAS REGISTRY NUMBER
COMMENTARY hide
136447-03-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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A8FJX8
UniProt
Manually annotated by BRENDA team
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A8FJX8
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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 + NAD+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADH + H+
show the reaction diagram
carboxynorspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+
show the reaction diagram
carboxyspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + putrescine + NADPH + H+
show the reaction diagram
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+
carboxynorspermidine + NADP+ + H2O
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-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+
carboxynorspermidine + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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conmpletely inactive unless NADPH or NADH are added, NADH is a much poorer cofactor than NADPH
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no evidence for activity being dependent on metal ions such as Ca2+, Mg2+, Fe3+, Fe2+, Cu+, Cu2+, Mn2+, and Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-diaminopropane
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10 mM, causes 10-20% inhibition of carboxynorspermidine formation
cadaverine
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10 mM, causes 10-20% inhibition of carboxynorspermidine formation
ethylenediamine
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10 mM, causes 10-20% inhibition of carboxynorspermidine formation
ethylmaleimide
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5 mM, in presence of 20 mM, 83% inhibition
iodoacetamide
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5 mM, in presence of 20 mM, 24% inhibition
NADP+
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5 mM, 51% inhibition
norspermidine
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10 mM, 10% inhibition
additional information
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no inhibitory effect of NAD+, ATP, and spermidine at 5 or 10 mM. No effect of 1 mM Na+ or K+. No evidence for inhibitory effect of metal cations such as Ca2+, Mg2+, Fe3+, Fe2+, Cu+, Cu2+, Mn2+, and Zn2+. EDTA, 1 mM no inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
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without addition 7% of the maximum activity detected in the purified enzyme, 14fold activiation is observed at 20 mM
additional information
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1 mM EDTA shows no stimulatory effect on enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.68
L-aspartic 4-semialdehyde
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pH 7.5, 37C, Vmax: 35 micromol/min/mg carboxynorspermidine
2.97
NADH
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pH 7.5, 37C, with a Vmax of 13.5 micromol carboxynorspermidine/min/mg protein formed
1.51
NADPH
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pH 7.5, 37C, with a Vmax of 31 micromol carboxynorspermidine/min/mg protein formed
additional information
additional information
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the Km for the Schiff base is 4.68 mM, the intermediate formed from L-aspartic 4-semialdehyde and 1,3-diaminopropane, which is reduced to carboxynorspermidine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0039
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addition of 5 mM norspermidine to the growth medium, 27% compared to the specific activity without addition, pH 7.5, 37C
0.0108
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addition of 5 mM spermidine to the growth medium, 74% compared to the specific activity without addition, pH 7.5, 37C
0.01455
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without addition of norspermidine or spermidine to the growth medium, pH 7.5, 37C
31
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micromol carboxynorspermidine/min-1/mg protein, pH 7.5, 37C
additional information
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in the presence of 5 mM nospermidine, specific activity is reduced by 70%
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.25 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.25 - 8
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18 and 85% of the maximal acticity at pH 6.25 and 8.0, respectively
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 45
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78 and 59% of the maximal activity at 30 and 45C, respectively, no activity at 50C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2 - 4.3
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isoelectric focusing and chromatofocusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45100
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2 * 45100, SDS-PAGE, indicates that the native enzyme is composed of two subunits of similar size
93500
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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the enzyme is unstable in buffers below pH 6.5, at pH 6.5 50% loss of activity is observed within 12 h at 4C
712623
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no significant stabilization by addition of NADPH. 1 mM DTT has a protective effect on the enzyme during purification and storage. Freezing and thawing results in almost complete loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, protein concentration of 1.6 mg/ml in 20 mM Tris-HCl, pH 7.5, 1 mM DTT and 0.02% NaN3, lost of about 15% of its activity after one week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity, yield 33%, 1800fold purified, ammonium sulfate precipitation, DEAE-Sepharose CL-6B, hydroxyapatite, and Blue Sepharose CL-6B chromatography
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information