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Literature summary for 7.2.2.12 extracted from

  • Zimmer, J.; Doyle, D.A.
    Phospholipid requirement and pH optimum for the in vitro enzymatic activity of the E. coli P-type ATPase ZntA (2006), Biochim. Biophys. Acta, 1758, 645-652.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
1,2-dimyristoyl-phosphatidylglycerol solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol Escherichia coli
1,2-dioleoyl-phosphatidylglycerol solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol Escherichia coli
1,2-dipalmitoyl-phosphatidylglycerol solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol Escherichia coli
1,2-distearoyl-phosphatidylglycerol solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol Escherichia coli
Phospholipid solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Synonyms

Synonyms Comment Organism
ATPase ZntA
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Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
-
Escherichia coli