Information on EC 4.1.1.96 - carboxynorspermidine decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.96
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RECOMMENDED NAME
GeneOntology No.
carboxynorspermidine decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carboxynorspermidine = bis(3-aminopropyl)amine + CO2
show the reaction diagram
(1)
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carboxyspermidine = spermidine + CO2
show the reaction diagram
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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Metabolic pathways
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norspermidine biosynthesis
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polyamine pathway
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SYSTEMATIC NAME
IUBMB Comments
carboxynorspermidine carboxy-lyase (bis(3-aminopropyl)amine-forming)
A pyridoxal 5'-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae [1]. The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro [3].
CAS REGISTRY NUMBER
COMMENTARY hide
74114-38-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
serotype O139
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Manually annotated by BRENDA team
serotype O139
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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
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
bis(3-aminopropyl)amine + CO2
show the reaction diagram
carboxyspermidine
spermidine + CO2
show the reaction diagram
L-ornithine
?
show the reaction diagram
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the enzyme also exhibits some activity with L-ornithine
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?
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
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe2+
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82% inhibition at 1 mM
Fe3+
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88% inhibition at 1 mM
Mn2+
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50% inhibition at 1 mM
Zn2+
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23% inhibition at 1 mM
additional information
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not inhibited by 2,3-diaminopropionic acid, 2,4-diaminobutyric acid, L-ornithine, L-lysine, Mg2+, Ca2+, Cu2+, Cu+, Na+ and K+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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maximum stimulation of activity at more than 5 mM dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.175 - 2.1
carboxynorspermidine
0.1 - 4.1
carboxyspermidine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58 - 20.1
carboxynorspermidine
0.24 - 3.2
carboxyspermidine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
74
carboxynorspermidine
Vibrio vulnificus
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pH and temperature not specified in the publication
5063
3.2
carboxyspermidine
Vibrio vulnificus
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pH and temperature not specified in the publication
7915
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
Mn2+
Vibrio alginolyticus
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at pH 8.3 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0077
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crude extract, at pH 8.3 and 37°C
0.023
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purified recombinant enzyme, in 20 mM Tris/HCl, pH 7.5, containing 1 mM dithiothreitol and 0.1 mM EDTA, at 37°C
24.1
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after 3130fold purification, at pH 8.3 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
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57% and 72% of the maximum activity are observed at pH 7.5 and 9.0, respectively
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 55
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75% and 51% of the maximum activity remains at 30°C and 45°C, respectively, but the activity decreases rapidly at temperatures above 55°C or below 20°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42008
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x * 42008, calculated from amino acid sequence
86000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-crystallized with 10 mM norspermidine, hanging drop vapor diffusion method, using 2.75 M ammonium sulfate, 0.1 M Bicine, pH 8.5
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing the purified preparation results in almost complete loss of activity. A substantial loss of activity (about 20%) is observed when the enzyme is dialysed for 12 h or stored at 4°C for 2 days without addition of EDTA
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, at pH 7.5 in the presence of dithiothreitol, EDTA and NaN, at least one month, the enzyme remains stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Sephacryl S-200 gel filtration, and hydroxyapatite column chromatography. The enzyme is greatly stabilized by the addition of both dithiothreitol and EDTA, but not pyridoxal 5'-phosphate, during purification
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Ni2+ affinity column chromatography and gel filtration
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nitrilotriacetic acid affinity resin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli HB101 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Show AA Sequence (1632 entries)
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