Information on EC 1.1.1.233 - N-acylmannosamine 1-dehydrogenase

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The expected taxonomic range for this enzyme is: Flavobacterium

EC NUMBER
COMMENTARY hide
1.1.1.233
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RECOMMENDED NAME
GeneOntology No.
N-acylmannosamine 1-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-acyl-D-mannosamine + NAD+ = N-acyl-D-mannosaminolactone + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
-
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reduction
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SYSTEMATIC NAME
IUBMB Comments
N-acyl-D-mannosamine:NAD+ 1-oxidoreductase
Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine. Highly specific.
CAS REGISTRY NUMBER
COMMENTARY hide
117698-08-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
show the reaction diagram
N-glycolyl-D-mannosamine + NAD+
N-glycolyl-D-mannosaminolactone + NADH
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
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor: NADP+, ferricyanide, 2,6-dichlorophenolindophenol, phenazine methosulfate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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slight inhibition
Cd2+
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slight inhibition
Cu2+
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slight inhibition
Hg2+
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strong inhibitor
Mn2+
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slight inhibition
Ni2+
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slight inhibition
SDS
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strong inhibitor
Zn2+
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slight inhibition
additional information
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no inhibition with metal-chelating or SH-group-blocking reagents, e.g. EDTA, 2,2'-bipyridyl, 8-hydroxyquinoline, PCMB
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
N-acetyl-D-mannosamine
13.3
N-Glycolyl-D-mannosamine
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0.41
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.13
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crude extract
340
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purified enzyme
545
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11.5
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27470
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calculated from amino acid sequence
29000
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SDS-PAGE
120000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of ligand-free and ManNAc- and NAD+-bound enzyme forms reveal a compact homotetramer having point 222 symmetry, formed by subunits presenting the characteristic SDR alpha3beta7alpha3 sandwich fold. A highly developed C-terminal tail used as a latch connecting nearby subunits stabilizes the tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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inactivation at 25°C after 16 h, gradually reversed to about 80% of original activity by shifting the pH back to 8.2 and keeping it at room temperature for 36 h
389505
7
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and below, more than 70% loss of activity
389505
8.5 - 9.5
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more stable than at pH 8.2 at 45°C, 10 min
389505
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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inactivation at pH 5.0 after 16 h, gradually reversed to about 80% of original activity by shifting the pH back to 8.2 and keeping it at room temperature for 36 h
42
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and below, stable for at least 10 min
50
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t1/2: 10 min
60
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complete inactivation after 10 min
64
the enzyme shows a high thermal stability in glycine buffer, Tm = 64°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by frequent freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified from Escherichia coli clone
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned and expressed under control of a lac-promoter in Escherichia coli JM109, the Escherichia coli transformants JM109(pNAM307) and JM109(pNAM308) show up to 200-fold higher activity than Flavobacterium sp.
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis