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Information on EC 1.1.1.350 - ureidoglycolate dehydrogenase (NAD+) and Organism(s) Escherichia coli and UniProt Accession P77555

for references in articles please use BRENDA:EC1.1.1.350
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EC Tree
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)+].
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This record set is specific for:
Escherichia coli
UNIPROT: P77555
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
(S)-ureidoglycolate dehydrogenase, AllD, ureidoglycolate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(S)-ureidoglycolate dehydrogenase
-
ureidoglycolate dehydrogenase
-
-
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)+].
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
-
-
-
?
(S)-ureidoglycolate + NAD+
oxalurate + NADH + H+
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
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
0.01 - 110
NAD+
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBUNIT
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
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team