Information on EC 1.1.1.350 - ureidoglycolate dehydrogenase (NAD+)

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
1.1.1.350
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RECOMMENDED NAME
GeneOntology No.
ureidoglycolate dehydrogenase (NAD+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-ureidoglycolate + NAD+ = oxalurate + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
allantoin degradation IV (anaerobic)
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allantoin degradation
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Purine metabolism
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Microbial metabolism in diverse environments
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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)+].
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
(S)-ureidoglycolate + NAD+
oxalurate + NADH + H+
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+
oxalurate + NADH + H+
show the reaction diagram
P77555
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
the enzyme selectively utilizes NAD+ as a cofactor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.06 - 16.94
(S)-ureidoglycolate
0.37 - 2.28
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.29 - 57.06
(S)-ureidoglycolate
0.02 - 62.39
NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 54.3
(S)-ureidoglycolate
1342
0.01 - 110
NAD+
7
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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