Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.22 - UDP-glucose 6-dehydrogenase and Organism(s) Caenorhabditis elegans and UniProt Accession Q19905

for references in articles please use BRENDA:EC1.1.1.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Also acts on UDP-alpha-D-2-deoxyglucose.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Caenorhabditis elegans
UNIPROT: Q19905
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-glucose dehydrogenase, udpgdh, udpgd, udp-glucose 6-dehydrogenase, uridine diphosphoglucose dehydrogenase, udpglucose dehydrogenase, udp-gdh, udp-glc dehydrogenase, udpg dehydrogenase, udp-glcdh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, uridine diphosphoglucose
-
-
-
-
Sugarless protein
-
-
-
-
UDP-alpha-D-glucose:NAD oxidoreductase
-
-
-
-
UDP-D-glucose dehydrogenase
-
-
-
-
UDP-Glc dehydrogenase
-
-
-
-
UDP-Glc DH
-
-
-
-
UDP-GlcDH
-
-
-
-
UDPG dehydrogenase
-
-
-
-
UDPG:NAD oxidoreductase
-
-
-
-
UDPGDH
-
-
-
-
UDPGlc dehydrogenase
-
-
-
-
UDPglucose dehydrogenase
-
-
-
-
UDPglucose:NAD+ oxidoreductase
-
-
-
-
uridine diphosphate D-glucose dehydrogenase
-
-
-
-
uridine diphosphate glucose dehydrogenase
-
-
-
-
uridine diphosphoglucose dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:NAD+ 6-oxidoreductase
Also acts on UDP-alpha-D-2-deoxyglucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-26-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.333
NAD+
0.055
UDP-alpha-D-glucose
Hill coefficient 1, pH 7.5, 25°C
0.2
UDP-glucose
pH 8.7, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
NAD+
Hill coefficient 0.8, pH 7.5, 25°C
1.23
UDP-alpha-D-glucose
pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069
UDP-xylose
pH 7.5, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
enzyme activity increases dramatically in a special subset of vulval cells during vulval morphogenesis
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UGDH_CAEEL
481
0
52755
Swiss-Prot
other Location (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of unliganded and UDP-xylose bound UGDH. The A109P substitution that differs human and Caenorhabditis elgans enzymes is accommodated by an Asn-to-Ser substitution at position 290. The allosteric transition is conserved in UGDH, and UDP-Xyl binding induces formation of the Eomega hexamer. The enzyme also exhibits hysteresis in progress curves and negative cooperativity with respect to NAD+ binding
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hwang, H.Y.; Horvitz, H.R.
The Caenorhabditis elegans vulval morphogenesis gene sqv-4 encodes a UDP-glucose dehydrogenase that is temporally and spatially regulated
Proc. Natl. Acad. Sci. USA
99
14224-14229
2002
Caenorhabditis elegans (Q19905), Caenorhabditis elegans
Manually annotated by BRENDA team
Beattie, N.R.; Keul, N.D.; Hicks Sirmans, T.N.; McDonald, W.E.; Talmadge, T.M.; Taujale, R.; Kannan, N.; Wood, Z.A.
Conservation of atypical allostery in C. elegans UDP-glucose dehydrogenase
ACS omega
4
16318-16329
2019
Caenorhabditis elegans (Q19905), Caenorhabditis elegans
Manually annotated by BRENDA team