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Information on EC 1.1.1.350 - ureidoglycolate dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.350
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.350 ureidoglycolate dehydrogenase (NAD+)
IUBMB Comments
Involved in catabolism of purines. The enzyme from the bacterium Escherichia coli is specific for NAD+ . cf. EC 1.1.1.154, ureidoglycolate dehydrogenase [NAD(P)+].
The expected taxonomic range for this enzyme is: Escherichia coli
showSynonyms
(S)-ureidoglycolate dehydrogenase, AllD, ureidoglycolate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AllD
ureidoglycolate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-ureidoglycolate + NAD+ = N-carbamoyl-2-oxoglycine + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
allantoin degradation IV (anaerobic)
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SYSTEMATIC NAME
IUBMB Comments
(S)-ureidoglycolate:NAD+ oxidoreductase
Involved in catabolism of purines. The enzyme from the bacterium Escherichia coli is specific for NAD+ [2]. cf. EC 1.1.1.154, ureidoglycolate dehydrogenase [NAD(P)+].
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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
(S)-ureidoglycolate + NAD+
oxalurate + NADH + H+
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate + NAD+
oxalurate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate + NAD+
oxalurate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-ureidoglycolate + NAD+
oxalurate + NADH + H+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.06
(S)-ureidoglycolate
wild type enzyme, pH and temperature not specified in the publication
5.27
(S)-ureidoglycolate
mutant enzyme D141A, pH and temperature not specified in the publication
5.84
(S)-ureidoglycolate
mutant enzyme D141N, pH and temperature not specified in the publication
10.75
(S)-ureidoglycolate
mutant enzyme S43A, pH and temperature not specified in the publication
11.47
(S)-ureidoglycolate
mutant enzyme R259A, pH and temperature not specified in the publication
12.38
(S)-ureidoglycolate
mutant enzyme S140A, pH and temperature not specified in the publication
13.15
(S)-ureidoglycolate
mutant enzyme M251A, pH and temperature not specified in the publication
14.13
(S)-ureidoglycolate
mutant enzyme D141E, pH and temperature not specified in the publication
16.82
(S)-ureidoglycolate
mutant enzyme Y52F, pH and temperature not specified in the publication
16.94
(S)-ureidoglycolate
mutant enzyme H44A, pH and temperature not specified in the publication
0.37
NAD+
mutant enzyme D141E, pH and temperature not specified in the publication
0.52
NAD+
mutant enzyme D141A, pH and temperature not specified in the publication
0.56
NAD+
wild type enzyme, pH and temperature not specified in the publication
0.65
NAD+
mutant enzyme H44A, pH and temperature not specified in the publication
0.81
NAD+
mutant enzyme D141N, pH and temperature not specified in the publication
0.93
NAD+
mutant enzyme M251A, pH and temperature not specified in the publication
1.26
NAD+
mutant enzyme Y52F, pH and temperature not specified in the publication
1.39
NAD+
mutant enzyme S140A, pH and temperature not specified in the publication
1.49
NAD+
mutant enzyme R259A, pH and temperature not specified in the publication
2.28
NAD+
mutant enzyme S43A, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.29
(S)-ureidoglycolate
mutant enzyme S140A, pH and temperature not specified in the publication
1.37
(S)-ureidoglycolate
mutant enzyme S43A, pH and temperature not specified in the publication
1.62
(S)-ureidoglycolate
mutant enzyme D141A, pH and temperature not specified in the publication
1.67
(S)-ureidoglycolate
mutant enzyme D141E, pH and temperature not specified in the publication
1.76
(S)-ureidoglycolate
mutant enzyme H44A, pH and temperature not specified in the publication
1.92
(S)-ureidoglycolate
mutant enzyme Y52F, pH and temperature not specified in the publication
1.97
(S)-ureidoglycolate
mutant enzyme D141N, pH and temperature not specified in the publication
11.98
(S)-ureidoglycolate
mutant enzyme R259A, pH and temperature not specified in the publication
45.98
(S)-ureidoglycolate
mutant enzyme M251A, pH and temperature not specified in the publication
57.06
(S)-ureidoglycolate
wild type enzyme, pH and temperature not specified in the publication
0.02
NAD+
mutant enzyme S140A, pH and temperature not specified in the publication
0.87
NAD+
mutant enzyme D141E, pH and temperature not specified in the publication
1.03
NAD+
mutant enzyme H44A, pH and temperature not specified in the publication
1.06
NAD+
mutant enzyme D141A, pH and temperature not specified in the publication
1.47
NAD+
mutant enzyme D141N, pH and temperature not specified in the publication
1.9
NAD+
mutant enzyme Y52F, pH and temperature not specified in the publication
2.51
NAD+
mutant enzyme S43A, pH and temperature not specified in the publication
9.29
NAD+
mutant enzyme R259A, pH and temperature not specified in the publication
30.65
NAD+
mutant enzyme M251A, pH and temperature not specified in the publication
62.39
NAD+
wild type enzyme, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
(S)-ureidoglycolate
mutant enzyme H44A, pH and temperature not specified in the publication
0.1
(S)-ureidoglycolate
mutant enzyme S140A, pH and temperature not specified in the publication
0.11
(S)-ureidoglycolate
mutant enzyme Y52F, pH and temperature not specified in the publication
0.12
(S)-ureidoglycolate
mutant enzyme D141E, pH and temperature not specified in the publication
0.13
(S)-ureidoglycolate
mutant enzyme S43A, pH and temperature not specified in the publication
0.31
(S)-ureidoglycolate
mutant enzyme D141A, pH and temperature not specified in the publication
0.34
(S)-ureidoglycolate
mutant enzyme D141N, pH and temperature not specified in the publication
1.04
(S)-ureidoglycolate
mutant enzyme R259A, pH and temperature not specified in the publication
3.49
(S)-ureidoglycolate
mutant enzyme M251A, pH and temperature not specified in the publication
54.3
(S)-ureidoglycolate
wild type enzyme, pH and temperature not specified in the publication
0.01
NAD+
mutant enzyme S140A, pH and temperature not specified in the publication
1.1
NAD+
mutant enzyme S43A, pH and temperature not specified in the publication
1.51
NAD+
mutant enzyme Y52F, pH and temperature not specified in the publication
1.6
NAD+
mutant enzyme H44A, pH and temperature not specified in the publication
1.81
NAD+
mutant enzyme D141N, pH and temperature not specified in the publication
2.04
NAD+
mutant enzyme D141A, pH and temperature not specified in the publication
2.35
NAD+
mutant enzyme D141E, pH and temperature not specified in the publication
6.23
NAD+
mutant enzyme R259A, pH and temperature not specified in the publication
32.9
NAD+
mutant enzyme M251A, pH and temperature not specified in the publication
110
NAD+
wild type enzyme, pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo form, in a binary complex with NADH cofactor, and in a ternary complex with NADH and glyoxylate, hanging drop vapor diffusion method, using 0.1 M MES (pH 6.0) and 4.0 M NaCl, at 22°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D141A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
D141E
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
D141N
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
H44A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
M251A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R259A
in the mutant enzyme R259A, the kcat value is approximately 21% that of the wild type enzyme, with about an 11fold increase in Km
S140A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
S43A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Y52F
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cusa, E.; Obradors, N.; Baldoma, L.; Badia, J.; Aguilar, J.
Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli
J. Bacteriol.
181
7479-7484
1999
Escherichia coli, Escherichia coli ECL1
brenda
Kim, M.I.; Shin, I.; Cho, S.; Lee, J.; Rhee, S.
Structural and functional insights into (S)-ureidoglycolate dehydrogenase, a metabolic branch point enzyme in nitrogen utilization
PLoS ONE
7
e52066
2012
Escherichia coli (P77555)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.350)
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