Literature summary extracted from
Iwata, S.; Kamata, K.; Yoshida, S.; Minowa, T.; Ohta, T.
T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control (1994), Nat. Struct. Biol., 1, 176-185.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.1.1.27 |
fructose 1,6-diphosphate |
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate |
Bifidobacterium longum |
|
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.1.1.27 |
mutant C210S |
Bifidobacterium longum |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.1.1.27 |
C210S |
crystallization of mutant enzyme |
Bifidobacterium longum |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.27 |
Bifidobacterium longum |
- |
- |
- |