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Literature summary for 1.1.1.233 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)

Crystallization (Comment) Organism
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)

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

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

Substrates and Products (Substrate)

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

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

Synonyms

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.4
-
-
Flavobacterium sp.

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Flavobacterium sp.

General Information

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