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Information on EC 1.5.1.24 - N5-(carboxyethyl)ornithine synthase
for references in articles please use BRENDA:EC1.5.1.24
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.1 With NAD+ or NADP+ as acceptor
1.5.1.24 N5-(carboxyethyl)ornithine synthase
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
n5-(carboxyethyl)ornithine synthase, cbo0515, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N(5)-(L-1-carboxyethyl)-L-ornithine:NADP(+) oxidoreductase
-
-
-
-
N5-(CE) ornithine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O = L-ornithine + pyruvate + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive condensation
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
129070-70-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-N-acetylornithine + pyruvate + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
D-lysine + pyruvate + NADPH + H+
? + NADP+ + H2O
Substrates: enzyme also reacts with D-isomer
Products: -
Products: -
?
D-ornithine + pyruvate + NADPH + H+
N5-(L-1-carboxyethyl)-D-ornithine + NADP+ + H2O
Substrates: enzyme also reacts with D-isomer
Products: -
Products: -
?
L-lysine + pyruvate + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
L-ornithine + 2-oxo-butanoic acid + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
L-ornithine + 3-fluoropyruvic acid + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
L-ornithine + 3-mercaptopyruvic acid + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
L-ornithine + glyoxylic acid + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
L-ornithine + methylglyoxal + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
L-ornithine + oxaloacetic acid + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
L-ornithine + pyruvate + NADPH + H+
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O
Substrates: highest reaction rate
Products: -
Products: -
?
N2-methylornithine + pyruvate + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
N6-hydroxy-L-lysine + pyruvate + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
O-(2-aminoethyl)-L-serine + pyruvate + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
ornithine + 3-fluoropyruvate + NADPH
N6-(1-carboxy-2-fluoroethyl)ornithine + NADP+ + H2O
-
Substrates: slight activity observed, about 15% of the rate found with pyruvate
Products: -
Products: -
?
S-(2-aminoethyl)-L- cysteine + pyruvate + NADPH + H+
? + NADP+ + H2O
Substrates: weak reaction rate
Products: -
Products: -
?
L-ornithine + pyruvate + NADPH
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
ir
L-ornithine + pyruvate + NADPH
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O
-
Substrates: pyruvic acid serves as an effective keto substrate for the condensation reaction
Products: -
Products: -
ir
L-ornithine + pyruvate + NADPH
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O
-
Substrates: pyruvic acid serves as an effective keto substrate for the condensation reaction
Products: -
Products: -
ir
L-ornithine + pyruvate + NADPH
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
ir
lysine + pyruvate + NADPH
N7-(1-carboxyethyl)lysine + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
ir
lysine + pyruvate + NADPH
N7-(1-carboxyethyl)lysine + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
high affinity for NADPH, NADH cannot replace NADPH, but nicotinamide hypoxanthine dinucleotide phosphate, reduced form, is an effective substitute for the natural cofactor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.5
L-ornithine
pH 7.5, temperature not specified in the publication
0.15
pyruvate
pH 7.5, temperature not specified in the publication, Vmax: 0.9 micromol/min/mg protein
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. lactis K1, formerly Streptococcus lactis K1
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CEO1_LACLA
Lactococcus lactis subsp. lactis (strain IL1403)
309
0
35008
Swiss-Prot
-
CEO_CLOBH
Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
317
0
35849
Swiss-Prot
-
A0A0E1L4H5_CLOBO
317
0
35837
TrEMBL
-
G6F9A4_LACLL
313
0
35541
TrEMBL
-
A0A2R7Y0S7_LACLL
37
0
4314
TrEMBL
-
A0A1E8EZY8_9CLOT
313
0
35726
TrEMBL
-
B1KVJ3_CLOBM
Clostridium botulinum (strain Loch Maree / Type A3)
317
0
35823
TrEMBL
-
A0A2N5WEI1_LACLL
312
0
35145
TrEMBL
-
A7GAS0_CLOBL
Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)
317
0
35837
TrEMBL
-
C1FSJ3_CLOBJ
Clostridium botulinum (strain Kyoto / Type A2)
317
0
35837
TrEMBL
-
D2BN02_LACLK
Lactococcus lactis subsp. lactis (strain KF147)
312
0
35224
TrEMBL
-
A0A2R7Y092_LACLL
52
0
6039
TrEMBL
-
B1IF27_CLOBK
Clostridium botulinum (strain Okra / Type B1)
317
0
35837
TrEMBL
-
D2BMN3_LACLK
Lactococcus lactis subsp. lactis (strain KF147)
307
0
34646
TrEMBL
-
A0A0B4W8G4_CLOBO
317
0
35826
TrEMBL
-
J7T280_CLOS1
Clostridium sporogenes (strain ATCC 15579)
317
0
35766
TrEMBL
-
A0A3F3A1L3_CLOB6
Clostridium botulinum (strain 657 / Type Ba4)
317
0
35837
TrEMBL
-
G6FCP7_LACLL
309
0
35008
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
141300
-
gel filtration, analytical ultracentrifugation, sedimentation equilibrium
38000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
4 * 34200, sedimentation equilibrium, 20°C, 3.5 M guanidine-HCl
tetramer
-
4 * 34700, sedimentation equilibrium, 20°C, 3.0 M guanidine-HCl
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
heating CEOS in absence of guanidine-HCl produces irreversible denaturation and loss in activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzymatic activity of CEOS is lost at guanidine-HCl concentrations from 0.5-1.2 M
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% glycerol, freezing and thawing results in loss of all enzymatic activity
-20°C, no significant loss of activity detected after 2 months of storage
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme purified from the overproducing strain Escherichia coli CEO571
-
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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
-
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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
synthesis
nutrition
-
industrially important organism used widely as a starter in the dairy industry
nutrition
-
industrially important organism used widely as a starter in the dairy industry
-
synthesis
-
enzymatic biosyntheses of amino acids instead of chemical syntheses provide an attractive alternative to the former procedures since they are efficient and simple to perform. N,N-dialkylation does not occur and the enzyme-catalyzed reactions are both regio-and stereochemically specific
synthesis
-
enzymatic biosyntheses of amino acids instead of chemical syntheses provide an attractive alternative to the former procedures since they are efficient and simple to perform. N,N-dialkylation does not occur and the enzyme-catalyzed reactions are both regio-and stereochemically specific
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thompson, J.
N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase from Streptococcus lactis. Purification and partial characterization
J. Biol. Chem.
264
9592-9601
1989
Lactococcus lactis
brenda
Donkersloot, J.A.; Thompson, J.
Simultaneous loss of N5-(carboxyethyl)ornithine synthase, nisin production, and sucrose-fermenting ability by Lactococcus lactis K1
J. Bacteriol.
172
4122-4126
1990
Lactococcus lactis
brenda
Thompson, J.; Nguyen, N.Y.; Sackett, D.L.; Donkersloot, J.A.
Transposon-encoded sucrose metabolism in Lactococcus lactis
J. Biol. Chem.
266
14573-14579
1991
Lactococcus lactis, Lactococcus lactis K1-23
brenda
Miller, S.P.F.; Donkersloot, J.A.; Thompson, J.
Enzymatic synthesis and characterization of N5-(carboxymethyl)-L-ornithine and N6-(carboxymethyl)-L-lysine
Amino Acids
6
189-198
1994
Lactococcus lactis
brenda
Donkersloot, J.A.; Thompson, J.
Cloning, expression, sequence analysis, and site-directed mutagenesis of the Tn5306-encoded N5-(carboxyethyl)ornithine synthase from Lactococcus lactis K1
J. Biol. Chem.
270
12226-12234
1995
Lactococcus lactis, Lactococcus lactis K1-23
brenda
Ruvinov, S.B.; Thompson, J.; Sackett, D.L.; Ginsburg, A.
Tetrameric N5-(L-1-carboxyethyl)-L-ornithine synthase: Guanidine-HCl-induced unfolding and a low temperature requirement for refolding
Arch. Biochem. Biophys.
371
115-123
1999
Lactococcus lactis
brenda
Sackett, D.L.; Ruvinov, S.B.; Thompson, J.
N5-(L-1-carboxyethyl)-L-ornithine synthase: Physical and spectral characterization of teh enzyme and its unusual low pKa fluorescent tyrosine residues
Protein Sci.
8
2121-2129
1999
Lactococcus lactis
brenda
Thompson, J.; Hill, K.K.; Smith, T.J.; Pikis, A.
The gene CBO0515 from Clostridium botulinum strain Hall A encodes the rare enzyme N5-(carboxyethyl) ornithine synthase, EC 1.5.1.24
J. Bacteriol.
192
1151-1155
2010
Clostridium botulinum (A5HZ59), Clostridium botulinum
brenda
EXTERNAL LINKS (specific for EC-Number 1.5.1.24)
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