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Information on EC 1.1.1.233 - N-acylmannosamine 1-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.233
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.233 N-acylmannosamine 1-dehydrogenase
IUBMB Comments
Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine. Highly specific.
The expected taxonomic range for this enzyme is: unclassified Flavobacterium
showSynonyms
namdh, nam-dh, n-acyl-d-mannosamine dehydrogenase, n-acetyl-d-mannosamine dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N-acetyl-D-mannosamine dehydrogenase
N-acyl-D-mannosamine dehydrogenase
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-
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N-acylmannosamine dehydrogenase
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NAM-DH
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-
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NAMDH
N-acetyl-D-mannosamine dehydrogenase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-acyl-D-mannosamine + NAD+ = N-acyl-D-mannosaminolactone + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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.
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CAS REGISTRY NUMBER
COMMENTARY
117698-08-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
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Substrates: -
Products: -
Products: -
?
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
-
Substrates: reaction in N-acetyl-D-mannosamine catabolism
Products: -
Products: -
?
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
Substrates: strict selectivity towards N-acetyl-D-mannosamine and NAD+
Products: -
Products: -
?
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
-
Substrates: reaction in N-acetyl-D-mannosamine catabolism
Products: -
Products: -
?
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
Substrates: strict selectivity towards N-acetyl-D-mannosamine and NAD+
Products: -
Products: -
?
N-glycolyl-D-mannosamine + NAD+
N-glycolyl-D-mannosaminolactone + NADH
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Substrates: oxidation at 62% the rate of N-acetyl-D-mannosamine oxidation
Products: -
Products: -
?
N-glycolyl-D-mannosamine + NAD+
N-glycolyl-D-mannosaminolactone + NADH
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Substrates: oxidation at 62% the rate of N-acetyl-D-mannosamine oxidation
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
-
Substrates: reaction in N-acetyl-D-mannosamine catabolism
Products: -
Products: -
?
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
Substrates: strict selectivity towards N-acetyl-D-mannosamine and NAD+
Products: -
Products: -
?
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
-
Substrates: reaction in N-acetyl-D-mannosamine catabolism
Products: -
Products: -
?
N-acetyl-D-mannosamine + NAD+
N-acetyl-D-mannosaminolactone + NADH + H+
Substrates: strict selectivity towards N-acetyl-D-mannosamine and NAD+
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no cofactor: NADP+, ferricyanide, 2,6-dichlorophenolindophenol, phenazine methosulfate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
IMAGE
1
N-acetyl-D-mannosamine
-
value unchanged by cloning and expression in E. coli JM109
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
the enzyme belongs to the SDR (short-chain dehydrogenase/reductase) superfamily
evolution
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the enzyme belongs to the SDR (short-chain dehydrogenase/reductase) superfamily
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physiological function
enzyme NAMDH catalyzes a rare NAD+-dependent oxidation of N-acetyl-D-mannosamine into N-acetylmannosamino-lactone, which spontaneously hydrolyses into N-acetylmannosaminic acid
physiological function
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enzyme NAMDH catalyzes a rare NAD+-dependent oxidation of N-acetyl-D-mannosamine into N-acetylmannosamino-lactone, which spontaneously hydrolyses into N-acetylmannosaminic acid
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
64
the enzyme shows a high thermal stability in glycine buffer, Tm = 64°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
LITERATURE
analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Horiuchi, T.; Kurokawa, T.
Purification and properties of N-acyl-D-mannosamine dehydrogenase from Flavobacterium sp. 141-8
J. Biochem.
104
466-471
1988
Flavobacterium sp., Flavobacterium sp. 141-8
brenda
Yamamoto-Otake, H.; Koyama, Y.; Horiuchi, T.; Nakano, E.
Cloning, sequencing, and expression of the N-acyl-D-mannosamine dehydrogenase gene from Flavobacterium sp. strain 141-8 in Escherichia coli
Appl. Environ. Microbiol.
57
1418-1422
1991
Flavobacterium sp.
brenda
Sola-Carvajal, A.; Gil-Ortiz, F.; Garcia-Carmona, F.; Rubio, V.; Sanchez-Ferrer, A.
Crystal structures and functional studies clarify substrate selectivity and catalytic residues for the unique orphan enzyme N-acetyl-D-mannosamine dehydrogenase
Biochem. J.
462
499-511
2014
Flavobacterium sp. (P22441), Flavobacterium sp. 141-8 (P22441)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.233)
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