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) Haloferax volcanii and UniProt Accession D4GYH5

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:
Haloferax volcanii
UNIPROT: D4GYH5
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: Haloferax volcanii
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
HVO_1531
UDP-glucose dehydrogenase
-
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-alpha-D-mannose + 2 NAD+ + H2O
UDP-alpha-D-mannuronate + 2 NADH + 2 H+
show the reaction diagram
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-D-galactose + 2 NAD+ + H2O
UDP-alpha-D-galacturonate + 2 NADH + 2 H+
show the reaction diagram
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
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
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
metabolism
in the Haloferax volcanii archaeal glycosylation pathway, Agl, responsible for the assembly and attachment of an Asn-linked pentasaccharide, enzyme AglM acts as a UDP-glucose dehydrogenase, converting UDP-glucose into UDP-glucuronic acid
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
550000
gel filtration at 2 M NaCl
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
12 * 47000, about, SDS-PAGE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant CBD- and poly-His-tagged enzyme by ultracentrifugation and nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aglM, recombinant expression of CBD-tagged and C-terminally poly-His-tagged enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yurist-Doutsch, S.; Magidovich, H.; Ventura, V.V.; Hitchen, P.G.; Dell, A.; Eichler, J.
N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM
Mol. Microbiol.
75
1047-1058
2010
Haloferax volcanii (D4GYH5), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GYH5)
Manually annotated by BRENDA team
Kandiba, L.; Eichler, J.
AglM and VNG1048G, two haloarchaeal UDP-glucose dehydrogenases, show different salt-related behaviors
Life
6
pii: E31
2016
Haloferax volcanii (D4GYH5), Haloferax volcanii, Halobacterium salinarum (Q9HQQ9), Halobacterium salinarum, Haloferax volcanii ATCC 29605 (D4GYH5), Halobacterium salinarum ATCC 700922 (Q9HQQ9)
Manually annotated by BRENDA team