Information on EC 1.1.1.336 - UDP-N-acetyl-D-mannosamine dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

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EC NUMBER
COMMENTARY hide
1.1.1.336
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RECOMMENDED NAME
GeneOntology No.
UDP-N-acetyl-D-mannosamine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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UDP-N-acetyl-alpha-D-mannosaminouronate biosynthesis
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metabolism of amino sugars and derivatives
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-mannosamine:NAD+ 6-oxidoreductase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme has no activity with NADP+.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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activation at low UDP-N-acetylmannosamine concentrations
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetylglucosamine
1.3 mM, 50% inhibition
N-acetylmannosamine
0.07 mM, 50% inhibition
UDP
0.5 mM, 50% inhibition
UDP-glucose
0.6 mM, 50% inhibition
UTP
1 mM, 50% inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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2 mM, maximum activation
N-acetylglucosamine 1-phosphate
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activation at low UDP-N-acetylmannosamine concentrations
tris-(2-carboxyethyl)phosphine hydrochloride
1 mM, about 25% increase in activity
additional information
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the presence of SH compounds is required for activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 0.57
NAD+
0.11 - 0.38
UDP-N-acetyl-alpha-D-mannosamine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
NAD+
Methanococcus maripaludis
Q6LZC3
pH 8.5, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5 - 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46100
2 * 46100, calculated
51400
4 * 50000, SDS-PAGE, 4 * 51400, calculated, including His-tag
92000
gel filtration
100000
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gel filtration
200000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 50000, SDS-PAGE, 4 * 51400, calculated, including His-tag
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme bound to the product UDP-N-acetyl-alpha-D-mannosaminuronate by X-ray diffraction to resolution of 1.55 A. Crystal structures reveal a tight dimeric polymer chains with product-bound in all the structures. The catalytic residues Cys258 and Lys204 are conserved. The Cys258 acts as catalytic nucleophile and Lys204 as acid/base catalyst. The product directly interacts with residues Arg211, Thr249, Arg244, Gly255, Arg289, Lys319 and Arg398. The SeMet-substituted enzyme is crystallized using microbatch sitting method under reservoir solution condition 10% (w/v) PEG 8000, 8% (v/v) ethylene glycol and 0.1 M HEPES, pH 7.5
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to 1.8 A resolution, space group P21
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 20 mM Tris-HCl, pH 7.9, 3 M KC1, 2 mM 2-mercaptoethanol, and 10% glycerol, storage without loss of activity for 2 weeks, presence of bovine serum albumin stabilizes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
gene is not able to complement a defect in the Escherichia coli homologue wecC
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Show AA Sequence (877 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.336)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)