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Literature summary for 2.5.1.55 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.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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Aquifex aeolicus

Protein Variants

Protein Variants Comment Organism
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

Metals/Ions Comment Organism Structure
Cd2+ the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+ Aquifex aeolicus
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
Zn2+ wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations Aquifex aeolicus

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus O66496
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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