Information on EC 1.5.1.28 - Opine dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.5.1.28
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RECOMMENDED NAME
GeneOntology No.
Opine dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD+ + H2O = L-2-aminopentanoic acid + pyruvate + NADH + H+
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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reduction
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-
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SYSTEMATIC NAME
IUBMB Comments
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate:NAD+ oxidoreductase (L-aminopentanoate-forming)
In the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate.
CAS REGISTRY NUMBER
COMMENTARY hide
108281-02-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 1C
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Manually annotated by BRENDA team
no activity in Amphimedon queenslandica
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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
(R,S)-2,3-Diaminopropionic acid + pyruvate + NADH
?
show the reaction diagram
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9.67% of the activity with S: (S)-norvaline
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-
?
(R,S)-3-Aminobutanoate + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(R,S)-3-aminobutanoate + NAD+
show the reaction diagram
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0.68% of the activity with (S)-norvaline
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-
?
(S)-2-aminobutyric acid + pyruvate + NADH
N-[1-(R)-(carboxy)ethyl]-(S)-2-aminobutyric acid + NAD+
show the reaction diagram
(S)-Norleucine + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-norleucine + NAD+
show the reaction diagram
(S)-Norvaline + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-norvaline + NAD+
show the reaction diagram
(S)-Phenylalaninol + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-phenylalaninol + NAD+
show the reaction diagram
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0.63% of the activity with (S)-norvaline
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-
?
(S)-Phenylglycine + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-phenylglycine + NAD+
show the reaction diagram
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4.4% of the activity with (S)-norvaline
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-
?
amino acid + pyruvate + NADH + H+
opine + NAD+ + H2O
show the reaction diagram
beta-Chloro-(S)-Ala + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-beta-chloroalanine + NAD+
show the reaction diagram
Gly + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Gly + NAD+
show the reaction diagram
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5.3% of the activity with L-Met
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r
L-Ala + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Ala + NAD+
show the reaction diagram
L-Asp + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Asp + NAD+
show the reaction diagram
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1.2% of the activity with L-Met
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r
L-Cys + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Cys + NAD+
show the reaction diagram
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39% of the activity with L-Met
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r
L-Ile + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Ile + NAD+
show the reaction diagram
L-Leu + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Leu + NAD+
show the reaction diagram
L-Met + 2-oxobutanoate + NADH
?
show the reaction diagram
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11% of the activity with pyruvate
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r
L-Met + 2-oxohexanoate + NADH
?
show the reaction diagram
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2.1% of the activity with pyruvate
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r
L-Met + glyoxylate + NADH
?
show the reaction diagram
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11% of the activity with pyruvate
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r
L-Met + hydroxypyruvate + NADH
?
show the reaction diagram
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6.1% of the activity with pyruvate
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r
L-Met + oxaloacetate + NADH
?
show the reaction diagram
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30% of the activity with pyruvate
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r
L-Met + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Met + NAD+
show the reaction diagram
L-Phe + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Phe + NAD+
show the reaction diagram
L-Ser + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Ser + NAD+
show the reaction diagram
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39% of the activity with L-Met
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r
L-Thr + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Thr + NAD+
show the reaction diagram
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50% of the activity with L-Met
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r
L-Val + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-Val + NAD+
show the reaction diagram
O-Acetyl-(S)-Ser + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(S)-O-acetyl-Ser + NAD+
show the reaction diagram
p-Phospho-(S)-Tyr + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-(R,S)-p-phospho-(S)-Tyr + NAD+
show the reaction diagram
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0.64% of the activity with (S)-norvaline
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?
phospho-(S)-Ser + pyruvate + NADH
N-[1-(R)-(Carboxy)ethyl]-phospho-Ser + NAD+
show the reaction diagram
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15.8% of the activity with (S)-norvaline
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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
amino acid + pyruvate + NADH + H+
opine + NAD+ + H2O
show the reaction diagram
additional information
?
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the physiological role of this enzyme may be the degradation of opines of plant origin to yield NADH rather than the synthesis of the opines. The products 2-keto acid and L-amino acid can support the growth of the microorganism
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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0.13 mM, complete inhibition
Ag+
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0.13 mM, complete inhibition
Cd2+
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0.13 mM, complete inhibition
Cu2+
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0.13 mM, complete inhibition
Hg2+
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0.13 mM, complete inhibition
N-[1-S-(Carboxy)ethyl]-(S)-Phe
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NEM
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0.13 mM, complete inhibition
Ni2+
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0.13 mM, complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.9
(R,S)-2,3-diaminopropionic acid
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pyruvate and NADH as cosubstrates
20
(S)-2-aminobutanoate
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pyruvate and NADH as cosubstrates
3.72
(S)-norleucine
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pyruvate and NADH as cosubstrates
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2.17
(S)-norvaline
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pyruvate and NADH as cosubstrates
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28
2-Oxohexanoate
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L-Met and NADH as cosubstrate
3.19
beta-chloro-(S)-alanine
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pyruvate and NADH as cosubstrates
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8.8
glyoxylate
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L-Met and NADH as cosubstrate
5.1
L-Ala
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pyruvate and NADH as cosubstrates
2.5
L-Cys
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pyruvate and NADH as cosubstrates
6.2
L-Ile
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pyruvate and NADH as cosubstrates
2.9
L-Leu
4.1
L-Met
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pyruvate and NADH as cosubstrates
7.5 - 8.7
L-Phe
28.3
L-phenylglycine
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pyruvate and NADH as cosubstrates
3.6
L-Ser
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pyruvate and NADH as cosubstrates
7.4
L-Thr
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pyruvate and NADH as cosubstrates
3
L-Val
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pyruvate and NADH as cosubstrates
5.94
O-acetyl-(S)-Ser
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pyruvate and NADH as cosubstrates
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8.7
O-phospho-(S)-Ser
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pyruvate and NADH as cosubstrates
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3.5
oxaloacetate
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L-Met and NADH as cosubstrate
3
pyruvate
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L-Met and NADH as cosubstrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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amine-forming reaction
10
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oxidative deamination
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
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30°C, 1 h less than 15% loss of activity
94167
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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pH 5.0-9.5, 1 h, less than 15% loss of activity
37
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pH 8.0, 10 min, stable
50
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pH 8.0, 10 min, 20% loss of activity
52
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pH 8.0, 10 min, 50% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
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expression in Escherichia coli
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