Information on EC 1.8.1.11 - asparagusate reductase

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The expected taxonomic range for this enzyme is: Asparagus officinalis

EC NUMBER
COMMENTARY hide
1.8.1.11
-
RECOMMENDED NAME
GeneOntology No.
asparagusate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3-mercapto-2-mercaptomethylpropanoate:NAD+ oxidoreductase
Also acts on lipoate.
CAS REGISTRY NUMBER
COMMENTARY hide
56126-52-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
asparagusate + NADH
dihydroasparagusate + NAD+
show the reaction diagram
asparagusic acid + NADH
dihydroasparagusate + NAD+
show the reaction diagram
lipoic acid + NADH
dihydrolipoic acid + NAD+
show the reaction diagram
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
asparagusate + NADH
dihydroasparagusate + NAD+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
flavoprotein, approximately 1 mol of FAD per mol of protein
NAD+
-
up to 0.2 mM, stimulates the reduction activity if NADH concentration is 0.2 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenite
-
low inhibition
asparagusic acid
-
inhibits lipoyl dehydrogenase activity
cetyltrimethyl ammonium bromide
-
affects lipoyl dehydrogenase activity
FAD
-
strongly inhibits the two reductase activities
iodoacetamide
-
low inhibition
N-ethylmaleimide
-
-
NAD+
-
inactivator during asparagusic acid reduction
p-chloromercuribenzoic acid
-
-
additional information
-
inhibitors indicate an involvement of protein disulfide linkage or thiol group in the catalytic site
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lecithin
-
drastic activation of lipoyl dehydrogenase activity, no activation of asparagusate dehydrogenase activity, enzyme II
NAD+
-
reduction of lipoic acid is activated
sodium dodecylsulfate
-
treatment of mitochondria with at 0.5% for 10-20 min, maximal solubilization of enzyme
Tween 80
-
drastic activation of lipoyl dehydrogenase activity, no activation of asparagusate dehydrogenase activity, enzyme II
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20 - 21.5
Asparagusate
-
enzyme I and II
20
asparagusic acid
-
-
0.8 - 0.9
K3Fe(CN)6
3 - 3.3
lipoate
-
enzyme I and II
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.064
-
enzyme/fraction I towards asparagusic acid
0.08323
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enzyme/fraction II towards asparagusic acid
0.1631
-
enzyme/fraction I towards lipoic acid
0.213
-
enzyme/fraction II towards lipoic acid
0.215
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enzyme/fraction II towards asparagusic acid
0.425
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enzyme/fraction I towards asparagusic acid
0.5464
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enzyme/fraction II towards lipoic acid
1.082
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enzyme/fraction I towards lipoic acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.25
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for K3Fe(CN)6 reduction
5.95
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
around, higher levels than other regions
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000 - 111000
112000
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
5 min, activity completely retained; above, gradual loss of lipoyl dehydrogenase activity, complete loss at 90°C
60 - 70
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5 min, 1.4-fold activation of asparagusate dehydrogenase activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA ion stabilizes the enzyme
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PO43- stabilizes the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 67 mM sodium phosphate, pH 7.0, no loss of activity for at least 1 month
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4°C, 67 mM sodium phosphate, pH 7.0, very unstable
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4°C, 67 mM sodium phosphate, pH 7.0, very unstable, complete loss of activity in two weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration, ion-exchange, copurification of enzyme I and II
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gel filtration, ion-exchange, ultracentrifugation, copurification of type I and II
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SDS-extraction, gel filtration, ion-exchange
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