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Literature summary extracted from

  • 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 (2014), Biochem. J., 462, 499-511.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.233 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 Flavobacterium sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.233 N-acetyl-D-mannosamine + NAD+ Flavobacterium sp. strict selectivity towards N-acetyl-D-mannosamine and NAD+ N-acetyl-D-mannosaminolactone + NADH + H+
-
 ?
1.1.1.233 N-acetyl-D-mannosamine + NAD+ Flavobacterium sp. 141-8 strict selectivity towards N-acetyl-D-mannosamine and NAD+ N-acetyl-D-mannosaminolactone + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.233 Flavobacterium sp. P22441 soil bacteroidete
-
1.1.1.233 Flavobacterium sp. 141-8 P22441 soil bacteroidete
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.233 N-acetyl-D-mannosamine + NAD+ strict selectivity towards N-acetyl-D-mannosamine and NAD+ Flavobacterium sp. N-acetyl-D-mannosaminolactone + NADH + H+
-
 ?
1.1.1.233 N-acetyl-D-mannosamine + NAD+ strict selectivity towards N-acetyl-D-mannosamine and NAD+ Flavobacterium sp. 141-8 N-acetyl-D-mannosaminolactone + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.233 homotetramer structure analysis of NAMDH-substrate complexes Flavobacterium sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.1.233 N-acetyl-D-mannosamine dehydrogenase
-
 Flavobacterium sp.
1.1.1.233 NAMDH
-
 Flavobacterium sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.233 64
-
 the enzyme shows a high thermal stability in glycine buffer, Tm = 64°C Flavobacterium sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.233 9.4
-
-
 Flavobacterium sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.233 NAD+
-
 Flavobacterium sp.

General Information

EC Number General Information Comment Organism
1.1.1.233 evolution the enzyme belongs to the SDR (short-chain dehydrogenase/reductase) superfamily Flavobacterium sp.
1.1.1.233 additional information catalytic tetrade Flavobacterium sp.
1.1.1.233 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 Flavobacterium sp.