Literature summary extracted from
Wang, J.; Duewel, H.S.; Stuckey, J.A.; Woodard, R.W.; Gatti, D.L.
Function of His185 in Aquifex aeolicus 3-deoxy-D-manno-octulosonate 8-phosphate synthase (2002), J. Mol. Biol., 324, 205-214.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.5.1.55 |
- |
Aquifex aeolicus |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.5.1.55 |
H185G |
mutation decreases the affinity of the enzyme to bind Fe2+, but not Zn2+. Maximal activity, about 8-10% of the wild-type activity is obtained when the native metal is replaced with Cd2+ |
Aquifex aeolicus |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.5.1.55 |
Cd2+ |
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+ |
Aquifex aeolicus |
|
2.5.1.55 |
Fe2+ |
wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations. Mutation H185G decreases the ability of the enzyme to bind Fe2+, but not Zn2+. Maximal activity, about 8-10% of the wild-type activity is obtained when the native metal is replaced with Cd2+ |
Aquifex aeolicus |
|
2.5.1.55 |
Zn2+ |
wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations |
Aquifex aeolicus |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.5.1.55 |
Aquifex aeolicus |
O66496 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.5.1.55 |
phosphoenolpyruvate + D-arabinose 5-phosphate |
His185 is necessary for the correct binding of phosphoenolpyruvate and of a catalytic water molecule |
Aquifex aeolicus |
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate |
- |
? |
|