Information on EC 1.1.1.154 - ureidoglycolate dehydrogenase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
1.1.1.154
-
RECOMMENDED NAME
GeneOntology No.
ureidoglycolate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-ureidoglycolate + NAD(P)+ = oxalureate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
allantoin degradation IV (anaerobic)
-
-
Purine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-ureidoglycolate:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
62213-62-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Arthrobacter allantoicus
-
-
-
Manually annotated by BRENDA team
-
-
-
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
(S)-ureidoglycolate + NAD(P)+
oxalureate + NAD(P)H
show the reaction diagram
Arthrobacter allantoicus
-
strong substrate specificity, involved in the degradation of allantoin to glyoxylate in microbes and lower animals
-
ir
(S)-ureidoglycolate + NAD+
oxalureate + NADH
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
(S)-ureidoglycolate + NAD(P)+
oxalureate + NAD(P)H
show the reaction diagram
Arthrobacter allantoicus
-
strong substrate specificity, involved in the degradation of allantoin to glyoxylate in microbes and lower animals
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
Arthrobacter allantoicus
-
-
NADP+
Arthrobacter allantoicus
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycolate
Arthrobacter allantoicus
-
18% inhibition at 17 mM
glyoxylate
Arthrobacter allantoicus
-
non-competitive inhibition, Ki: 83 mM
L-lactate
Arthrobacter allantoicus
-
10% inhibition at 17 mM
Zn2+
Arthrobacter allantoicus
-
40% inhibition at 0.5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.1
(R,S)-ureidoglycolate
Arthrobacter allantoicus
-
-
1.06 - 16.94
(S)-ureidoglycolate
0.37 - 2.28
NAD+
0.1
NADP+
Arthrobacter allantoicus
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.29 - 57
(S)-ureidoglycolate
0.02 - 62
NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 54
(S)-ureidoglycolate
1342
0.01 - 110
NAD+
7
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.6
Arthrobacter allantoicus
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.4
Arthrobacter allantoicus
-
sensitive to ionic strength
8.1
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Arthrobacter allantoicus
-
-
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of AllD in its apo form is determined at 2.13 A resolution, as well as a binary complex at 1.64 A resolution with the NADH cofactor, and a ternary complex at 1.77 A resolution with NADH and glyoxylate, a product yielded from the spontaneous degradation of oxalurate
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
Arthrobacter allantoicus
-
decrease of activity below
286034
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
Arthrobacter allantoicus
-
unstable above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
incubation with 30% glycerol at 4°C for 3 h stabilizes activity
Arthrobacter allantoicus
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Arthrobacter allantoicus
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expresed as a His-tagged fusion protein in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D141A
-
Km ((S)-ureidoglycolate) increased, kcat (S-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) similar to wo wild-type
D141E
-
Km ((S)-ureidoglycolate) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) decreased compared to wild-type
D141N
-
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
H116A
-
mutant(S)-ureidoglycolate shows no activity
H44A
-
Km ((S)-ureidoglycolate) increased, kcat (S-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) equal to wild-type
M251A
-
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
R259A
-
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
R48A
-
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
S140A
-
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
S43A
-
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Y52F
-
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
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