EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.367 | in an open form of the apoenzyme. Enzyme CapF is a homodimer displaying a characteristic dumb-bell-shaped architecture composed of two domains. The N-terminal domain (residues 1-252) adopts a Rossmann fold belonging to the short-chain dehydrogenase/reductase family of proteins. The C-terminal domain (residues 252-369) displays a standard cupin fold with a Zn2+ ion bound deep in the binding pocket of the beta-barrel. The cupin domain is necessary for the C3-epimerization of UDP-4-hexulose. The N-terminal domain catalyses the NADPH-dependent reduction of the intermediate species generated by the cupin domain. A thermodynamic switch governs the attachment and release of the coenzyme NADPH during each catalytic cycle. suggesting that the binding of coenzyme to CapF facilitates a disorder-to-order transition in the catalytic loop of the reductase (N-terminal) domain | Staphylococcus aureus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.367 | F297Y | mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity | Staphylococcus aureus |
1.1.1.367 | H290L | mutation in he coordination sphere of Zn2+. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product | Staphylococcus aureus |
1.1.1.367 | H337L | mutant displays diminished thermal stability | Staphylococcus aureus |
1.1.1.367 | S94A/Y103A | catalytic site of the short-chain dehydrogenase/reductase domain. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product. Addition of the reductase domain rescue the enzymatic activity | Staphylococcus aureus |
1.1.1.367 | T364Y F297Y | mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity | Staphylococcus aureus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.367 | Zn2+ | the C-terminal domain of the enzyme displays a standard cupin fold with a Zn2+ ion bound deep in the binding pocket of the beta-barrel | Staphylococcus aureus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.367 | Staphylococcus aureus | A0A0H3JP37 | - |
- |
1.1.1.367 | Staphylococcus aureus ATCC 700699 | A0A0H3JP37 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.367 | UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+ | - |
Staphylococcus aureus | UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+ | reaction proceeeds via the intermediate UDP-2-acetamido-2,6-dideoxy-beta-L-lyxo-4-hexulose | ? | |
1.1.1.367 | UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+ | - |
Staphylococcus aureus ATCC 700699 | UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+ | reaction proceeeds via the intermediate UDP-2-acetamido-2,6-dideoxy-beta-L-lyxo-4-hexulose | ? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.367 | Cap5F | - |
Staphylococcus aureus |
1.1.1.367 | CapF | - |
Staphylococcus aureus |
1.1.1.367 | capsular polysaccharide synthesis enzyme | - |
Staphylococcus aureus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.367 | NADPH | cofactor is essential only for the reduction reaction, NAPH binding is enthalpy-driven | Staphylococcus aureus |