Crystallization (Comment) | Organism |
---|---|
hanging-drop vapor-diffusion method | Oryctolagus cuniculus |
Protein Variants | Comment | Organism |
---|---|---|
D128V | mutation, mimicking the clinically important D128G mutation in humans | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-bisphosphate | Oryctolagus cuniculus | aldolase is involved in the metabolism of fructose, converting fructose 1-phosphate to dihydroxyacetone phosphate and glyceraldehyde | dihydroxyacetone phosphate + glyceraldehyde 3-phosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | P00883 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-bisphosphate | aldolase is involved in the metabolism of fructose, converting fructose 1-phosphate to dihydroxyacetone phosphate and glyceraldehyde | Oryctolagus cuniculus | dihydroxyacetone phosphate + glyceraldehyde 3-phosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | rabbit muscle D128V aldolase. The D128V mutation causes aldolase to lose intermolecular contacts with the neighbouring subunit at one of the two interfaces of the tetramer | Oryctolagus cuniculus |
tetramer | wild-type | Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
fructose-1,6-bisphosphate aldolase A | - |
Oryctolagus cuniculus |