Information on EC 1.1.1.374 - UDP-N-acetylglucosamine 3-dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Methanococcus maripaludis

EC NUMBER
COMMENTARY hide
1.1.1.374
-
RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine 3-dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + NAD+ = UDP-2-acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose + NADH + H+
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:NAD+ 3-oxidoreductase
The enzyme from the archaeon Methanococcus maripaludis is activated by KCl (200 mM).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the biosynthesis of glycan component sugars
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + NAD+
UDP-2-acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose + 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
UDP-N-acetyl-alpha-D-glucosamine + NAD+
UDP-2-acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose + NADH + H+
show the reaction diagram
Q6M0B9
the enzyme is involved in the biosynthesis of glycan component sugars
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
activity is 85% lower in the absence of KCl as compared with reactions containing 200 mM KCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UDP
2 mM, reduces activity by 50%
UDP-alpha-D-glucose
2 mM, reduces activity by 50%
UDP-alpha-N-acetyl-D-galactosamine
3 mM, reduces activity by 50%
-
additional information
N-acetyl-D-glucosamine, D-glucose, and D-glucosamine do not inhibit the reaction at 3-mM concentrations
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.99
NAD+
Methanococcus maripaludis
Q6M0B9
pH 8.5, 37°C
0.9
UDP-N-acetyl-alpha-D-glucosamine
Methanococcus maripaludis
Q6M0B9
pH 8.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.5
NAD+
Methanococcus maripaludis
Q6M0B9
pH 8.5, 37°C
7
5
UDP-N-acetyl-alpha-D-glucosamine
Methanococcus maripaludis
Q6M0B9
pH 8.5, 37°C
1424
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
305000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 39000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for at least several weeks in 20% glycerol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
high-throughput chromatographic analysis of UDP–GlcNAc in a complex matrix of deproteinized cell extract