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
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
141-8
-
-
Manually annotated by BRENDA team
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
NAD+
-
specific for
additional information
-
no cofactor: NADP+, ferricyanide, 2,6-dichlorophenolindophenol, phenazine methosulfate
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
-
slight inhibition
Cd2+
-
slight inhibition
Cu2+
-
slight inhibition
Hg2+
-
strong inhibitor
Mn2+
-
slight inhibition
Ni2+
-
slight inhibition
SDS
-
strong inhibitor
Zn2+
-
slight inhibition
additional information
-
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
-
-
0.41
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.13
-
crude extract
340
-
purified enzyme
545
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11.5
-
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27470
-
calculated from amino acid sequence
29000
-
SDS-PAGE
120000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
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
-
and below, more than 70% loss of activity
389505
8.5 - 9.5
-
more stable than at pH 8.2 at 45°C, 10 min
389505
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
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
-
and below, stable for at least 10 min
50
-
t1/2: 10 min
60
-
complete inactivation after 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by frequent freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified from Escherichia coli clone
-
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.
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis