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Information on EC 1.1.1.154 - ureidoglycolate dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.154
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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
1.1.1.154 ureidoglycolate dehydrogenase [NAD(P)+]
IUBMB Comments
Involved in catabolism of purines. The enzyme from the bacterium Arthrobacter allantoicus can use both NAD+ and NADP+ with similar activity. cf. EC 1.1.1.350, ureidoglycolate dehydrogenase (NAD+).
The expected taxonomic range for this enzyme is: Escherichia coli
- 1.1.1.154
- glucose-6-phosphate
-
hemolytic
-
anemia
-
hyperbilirubinemia
-
nonspherocytic
-
favism
- primaquine
-
tribal
showSynonyms
ureidoglycolate dehydrogenase, (s)-ureidoglycolate dehydrogenase, more
top
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S-ureidoglycolate dehydrogenase
-
-
-
-
ureidoglycolate dehydrogenase
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-ureidoglycolate + NAD(P)+ = N-carbamoyl-2-oxoglycine + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(S)-ureidoglycolate:NAD(P)+ oxidoreductase
Involved in catabolism of purines. The enzyme from the bacterium Arthrobacter allantoicus can use both NAD+ and NADP+ with similar activity. cf. EC 1.1.1.350, ureidoglycolate dehydrogenase (NAD+).
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CAS REGISTRY NUMBER
COMMENTARY
62213-62-1
-
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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
(R,S)-ureidoglycolate + NAD+
oxalureate + NADH + H+
Arthrobacter allantoicus
-
Substrates: -
Products: -
Products: -
r
(S)-ureidoglycolate + NAD(P)+
oxalureate + NAD(P)H
Arthrobacter allantoicus
-
Substrates: strong substrate specificity, involved in the degradation of allantoin to glyoxylate in microbes and lower animals
Products: -
Products: -
ir
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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(P)+
oxalureate + NAD(P)H
Arthrobacter allantoicus
-
Substrates: strong substrate specificity, involved in the degradation of allantoin to glyoxylate in microbes and lower animals
Products: -
Products: -
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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). ALLD_ECOLI
Escherichia coli (strain K12)
349
0
37967
Swiss-Prot
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
Van der Drift, C.; van Helvoort, P.E.M.; Vogels, G.D.
S-ureidoglycolate dehydrogenase: Purification and properties
Arch. Biochem. Biophys.
145
465-469
1971
Arthrobacter allantoicus
brenda
Rothe, M.; Alpert, C.; Loh, G.; Blaut, M.
Novel insights into E. colis hexuronate metabolism: KduI facilitates the conversion of galacturonate and glucuronate under osmotic stress conditions
PLoS ONE
8
e56906
2013
Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.154)
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