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. |
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+ | - |
? |
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 | - |
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+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.233 | homotetramer | structure analysis of NAMDH-substrate complexes | Flavobacterium sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.233 | N-acetyl-D-mannosamine dehydrogenase | - |
Flavobacterium sp. |
1.1.1.233 | NAMDH | - |
Flavobacterium sp. |
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. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.233 | 9.4 | - |
- |
Flavobacterium sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.233 | NAD+ | - |
Flavobacterium sp. |
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. |