Information on EC 1.5.1.24 - N5-(carboxyethyl)ornithine synthase

Word Map on EC 1.5.1.24
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.24
-
RECOMMENDED NAME
GeneOntology No.
N5-(carboxyethyl)ornithine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O = L-ornithine + pyruvate + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase (L-ornithine-forming)
In the reverse direction, L-lysine can act instead of L-ornithine, but more slowly. Acts on the amino group. cf. EC 1.5.1.16, D-lysopine dehydrogenase.
CAS REGISTRY NUMBER
COMMENTARY hide
129070-70-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K1-23, formerly Streptococcus lactis K1-23
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-N-acetylornithine + pyruvate + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
D-lysine + pyruvate + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
enzyme also reacts with D-isomer
-
-
?
D-ornithine + pyruvate + NADPH + H+
N5-(L-1-carboxyethyl)-D-ornithine + NADP+ + H2O
show the reaction diagram
enzyme also reacts with D-isomer
-
-
?
L-lysine + pyruvate + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
L-ornithine + 2-oxo-butanoic acid + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
L-ornithine + 3-fluoropyruvic acid + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
L-ornithine + 3-mercaptopyruvic acid + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
L-ornithine + glyoxylic acid + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
L-ornithine + methylglyoxal + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
L-ornithine + oxaloacetic acid + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
L-ornithine + pyruvate + NADPH
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O
show the reaction diagram
L-ornithine + pyruvate + NADPH + H+
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O
show the reaction diagram
highest reaction rate
-
-
?
lysine + pyruvate + NADPH
N7-(1-carboxyethyl)lysine + NADP+ + H2O
show the reaction diagram
N2-methylornithine + pyruvate + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
N6-hydroxy-L-lysine + pyruvate + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
O-(2-aminoethyl)-L-serine + pyruvate + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
ornithine + 3-fluoropyruvate + NADPH
N6-(1-carboxy-2-fluoroethyl)ornithine + NADP+ + H2O
show the reaction diagram
-
slight activity observed, about 15% of the rate found with pyruvate
-
-
?
S-(2-aminoethyl)-L- cysteine + pyruvate + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
weak reaction rate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
gamma-glutamyl peptide
-
-
-
N5-(L-1-carboxyethyl)-L-ornithine
-
-
additional information
-
anti-NADP+ oxidoreductase IgG
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29.5
L-ornithine
pH 7.5, temperature not specified in the publication
18.2
lysine
-
-
0.0066 - 2.95
NADPH
3.3
ornithine
-
-
0.15
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
pH 7.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35320
-
deduced from amino acid sequence
35850
calculated from cDNA
37000 - 38000
-
immunoblot analysis
39200
-
calculated from amino acid sequence
78000
-
gel filtration
125000
gel filtration
127500
-
sedimentation equilibrium at 20C, 3.0 M guanidine-HCl
135900
-
sedimentation equilibrium at 20C, 3.0 M guanidine-HCl
136900
-
sedimentation equilibrium at 20C
137000
-
XLA
138900
-
sedimentation equilibrium at 20C, 3.5 M guanidine-HCl
140000
-
native PAGE
141300
-
gel filtration, analytical ultracentrifugation, sedimentation equilibrium
145700
-
sedimentation equilibrium at 4C
146700
-
sedimentation equilibrium at 20C, 3.5 M guanidine-HCl
150000
-
PAGE, hight pressure liquid chromatography, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 38000, SDS-PAGE
homotetramer
in solution, gel filtration
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
stable to heating for 10 min
55
-
heating CEOS in absence of guanidine-HCl produces irreversible denaturation and loss in activity
60
-
rapidly inactivated by heating at
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 20% glycerol stabilizes the enzyme
-
enzymatic activity of CEOS is lost at guanidine-HCl concentrations from 0.5-1.2 M
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20% glycerol, freezing and thawing results in loss of all enzymatic activity
-20C, 25% (NH4)2SO4, several months, no loss in activity
-20C, no significant loss of activity detected after 2 months of storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme purified from the overproducing strain Escherichia coli CEO571
-
using anion-exchange and phosphocellulose P-11 chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ceo gene encoding N5-(carboxyethyl)ornithine synthase isolated from transposon Tn5306 of Lactococcus lactis K1 cloned and sequenced, expression in Escherichia coli CEO571
-
ceo gene encoding N5-(carboxyethyl)ornithine synthase isolated from transposon Tn5306 of Lactococcus lactis K1 cloned and sequenced, expression in Escherichia coli CEO571; gene ceo, encoding the tetrameric enzyme, cloned and sequenced, plasmid p493 containing ceo transformed into Escherichia coli TG1
-
expressed in Escherichia coli
gene ceo, encoding the tetrameric enzyme, cloned and sequenced, plasmid p493 containing ceo transformed into Escherichia coli TG1
-
structural gene for N5-CEO synthase is located on the chromosome of Lactococcus lactis K1
-
transposon Tn5306 encodes ceo
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D114A
severe reduction (higher than 95%) in enzymatic activity
E13A
severe reduction (higher than 95%) in enzymatic activity
H92L
severe reduction (higher than 95%) in enzymatic activity
K71R
severe reduction (higher than 95%) in enzymatic activity
R15K
severe reduction (higher than 95%) in enzymatic activity
W90S
severe reduction (higher than 95%) in enzymatic activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
synthesis