Crystallization (Comment) | Organism |
---|---|
apo W89A and its ternary complex with Mg-alpha,beta-methyleneadenosine triphosphate and 6-hydroxymethyl-7,8-dihydropterin are crystallized at 19°C using the hanging-drop vapor-diffusion technique. The structure of the ternary complex is determined at 1.25 A resolution | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
R84A | little changes in the dissociation constants and kinetic constants of the HPPK-catalyzed reaction | Escherichia coli |
W89A | mutation increases the Kd for the binding of MgATP2- by a factor of 3, whereas the Kd for 6-hydroxymethyl-7,8-dihydropterin increases by a factor of 6, which is due to the increase in the dissociation rate constant. The mutation decreases the rate constant for the chemical step of the forward reaction by a factor of 15 and the rate constant for the chemical step of the reverse reaction by a factor of 25. The crystal structures of W89A show that W89A has different conformations in loops 2 and 3, but the critical catalytic residues are positioned for catalysis | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P26281 | - |
- |
Purification (Comment) | Organism |
---|---|
HPPK-glutathione S-transferase fusion proteins | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 6-hydroxymethyl-7,8-dihydropteridine | - |
Escherichia coli | AMP + 7,8-dihydro-6-(diphosphooxymethyl)pteridine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase | - |
Escherichia coli |
HPPK | - |
Escherichia coli |