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Literature summary extracted from

  • Behrens, M.; Schreiber, W.; Durre, P.
    The high-affinity K-translocating ATPase complex from Clostridium acetobutylicum consists of six subunits (2001), Anaerobe, 7, 159-169.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.6 expression in Escherichia coli Clostridium acetobutylicum

Protein Variants

EC Number Protein Variants Comment Organism
7.2.2.6 DELTAkdpX truncation of the kdpX gene leads to a less efficient K+-pump than wild-type Clostridium acetobutylicum
7.2.2.6 DELTAkdpY truncation of the kdpY gene has a significant impact on the growth of the Escherichia coli mutant TK2205, which is unable to grow at low potassium concentrations Clostridium acetobutylicum
7.2.2.6 DELTAkdpZ truncation of the kdpZ gene has a significant impact on the growth of the Escherichia coli mutant TK2205, which is unable to grow at low potassium concentrations Clostridium acetobutylicum
7.2.2.6 DELTAkdpZY loss of K+ transport Clostridium acetobutylicum

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.6 Clostridium acetobutylicum
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.2.2.6 285
-
 wild-type Clostridium acetobutylicum
7.2.2.6 453
-
 DELTAkdpZY Clostridium acetobutylicum
7.2.2.6 597
-
 wild-type with His-tag Clostridium acetobutylicum
7.2.2.6 793
-
 DELTAkdpX Clostridium acetobutylicum
7.2.2.6 3102
-
 DELTAkdpY Clostridium acetobutylicum
7.2.2.6 4073
-
 DELTAkdpZ Clostridium acetobutylicum