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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
cansdh, carboxynorspermidine dehydrogenase,
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carboxynorspermidine synthase
C-NSPD synthase
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carboxynorspermidine synthase
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carboxynorspermidine synthase
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L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+ = carboxynorspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+ = carboxynorspermidine + NADP+ + H2O
i.e. (3-((3-aminopropyl)amino)propyl)carbamate (carboxynorspermidine) and (2S)-2-amino-4-oxobutanoate (L-aspartic 4-semialdehyde) via a nicotinamide-nucleotide reduction of the Schiff base H2N(CH2)3=CHCH2CH(NH2)COOH, formed from L-aspartic beta-semialdehyde, an intermediate in the novel pathway for norspermidine biosynthesis
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L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+ = carboxynorspermidine + NADP+ + H2O
i.e. (3-((3-aminopropyl)amino)propyl)carbamate (carboxynorspermidine) and (2S)-2-amino-4-oxobutanoate (L-aspartic 4-semialdehyde) via a nicotinamide-nucleotide reduction of the Schiff base H2N(CH2)3=CHCH2CH(NH2)COOH, formed from L-aspartic beta-semialdehyde, an intermediate in the novel pathway for norspermidine biosynthesis
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L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+ = carboxynorspermidine + NADP+ + H2O
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(3-((3-aminopropyl)amino)propyl)carbamate:NADP+ oxidase
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carboxynorspermidine + NAD+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADH + H+
carboxynorspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+
carboxyspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + putrescine + NADPH + H+
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+
carboxynorspermidine + NADP+ + H2O
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additional information
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carboxynorspermidine + NAD+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADH + H+
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NADH is a much poorer cofactor than NADPH
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carboxynorspermidine + NAD+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADH + H+
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NADH is a much poorer cofactor than NADPH
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carboxynorspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+
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i.e. (3-((3-aminopropyl)amino)propyl)carbamate, incubation of the purified enzyme in the range of pH 6-8, with cofactor NADP+ or NAD+ concentrations up to 5 mM and substrate concentrations of carboxynorspermidine up to 10 mM, no reversible activity is observed
i.e. (2S)-2-amino-4-oxobutanoate
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carboxynorspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+
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i.e. (3-((3-aminopropyl)amino)propyl)carbamate, incubation of the purified enzyme in the range of pH 6-8, with cofactor NADP+ or NAD+ concentrations up to 5 mM and substrate concentrations of carboxynorspermidine up to 10 mM, no reversible activity is observed
i.e. (2S)-2-amino-4-oxobutanoate
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carboxyspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + putrescine + NADPH + H+
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i.e. 3-[(4-aminobutyl)amino]-L-alanine, slightly active with putrescine, ca. 7% of the rate compared to 1,3-diaminopropane
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carboxyspermidine + NADP+ + H2O
L-aspartic 4-semialdehyde + putrescine + NADPH + H+
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i.e. 3-[(4-aminobutyl)amino]-L-alanine, slightly active with putrescine, ca. 7% of the rate compared to 1,3-diaminopropane
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additional information
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no activity with ethylenediamine, cadaverine, and D-aspartic beta-semialdehyde
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additional information
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no activity with ethylenediamine, cadaverine, and D-aspartic beta-semialdehyde
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L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+
carboxynorspermidine + NADP+ + H2O
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NADH
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conmpletely inactive unless NADPH or NADH are added, NADH is a much poorer cofactor than NADPH
NADPH
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NADPH
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conmpletely inactive unless NADPH or NADH are added, NADH is a much poorer cofactor than NADPH
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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+
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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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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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4.68
L-aspartic 4-semialdehyde
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pH 7.5, 37°C, Vmax: 35 micromol/min/mg carboxynorspermidine
2.97
NADH
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pH 7.5, 37°C, with a Vmax of 13.5 micromol carboxynorspermidine/min/mg protein formed
1.51
NADPH
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pH 7.5, 37°C, 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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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, 37°C
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, 37°C
0.01455
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without addition of norspermidine or spermidine to the growth medium, pH 7.5, 37°C
31
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micromol carboxynorspermidine/min-1/mg protein, pH 7.5, 37°C
additional information
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in the presence of 5 mM nospermidine, specific activity is reduced by 70%
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6.25 - 8
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18 and 85% of the maximal acticity at pH 6.25 and 8.0, respectively
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30 - 45
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78 and 59% of the maximal activity at 30 and 45°C, respectively, no activity at 50°C
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4.2 - 4.3
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isoelectric focusing and chromatofocusing
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UniProt
brenda
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brenda
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evolution
the enzyme is found in diverse bacterial phyla, overview. orthologues encoding carboxyspermidine dehydrogenase and carboxyspermidine decarboxylase are found clustered with an array of diverse putrescine biosynthetic genes in different bacterial genomes, consistent with a role in spermidine, rather than sym-norspermidine biosynthesis
malfunction
the CASDH gene deletion strain grows normally
physiological function
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carboxynorspermidine synthase participates in the novel pathway for norspermidine biosynthesis, with two other enzymes, 2,4-diamonobutyrate deacroxylase and carboxynorspermidine decarboxylase
physiological function
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carboxynorspermidine synthase participates in the novel pathway for norspermidine biosynthesis, with two other enzymes, 2,4-diamonobutyrate deacroxylase and carboxynorspermidine decarboxylase
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A0A1J6U6V7_CAMJU
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44848
TrEMBL
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45100
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2 * 45100, SDS-PAGE, indicates that the native enzyme is composed of two subunits of similar size
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dimer
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2 * 45100, SDS-PAGE, indicates that the native enzyme is composed of two subunits of similar size
dimer
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2 * 45100, SDS-PAGE, indicates that the native enzyme is composed of two subunits of similar size
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additional information
deletion of the gene encoding carboxynorspermidine dehydrogenase. The CASDH gene deletion strain grows normally
additional information
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deletion of the gene encoding carboxynorspermidine dehydrogenase. The CASDH gene deletion strain grows normally
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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 4°C
712623
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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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4°C, 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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to homogeneity, yield 33%, 1800fold purified, ammonium sulfate precipitation, DEAE-Sepharose CL-6B, hydroxyapatite, and Blue Sepharose CL-6B chromatography
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Nakao, H.; Shinoda, S.; Yamamoto, S.
Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine inVibrio alginolyticus
J. Gen. Microbiol.
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1737-1742
1991
Vibrio alginolyticus
brenda
Hanfrey, C.C.; Pearson, B.M.; Hazeldine, S.; Lee, J.; Gaskin, D.J.; Woster, P.M.; Phillips, M.A.; Michael, A.J.
Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota
J. Biol. Chem.
286
43301-43312
2011
Campylobacter jejuni (A0A1J6U6V7), Campylobacter jejuni
brenda
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1.4.1.B4 carboxynorspermidine dehydrogenase
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