Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.2.2.6 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)

Cloned (Comment) Organism
expression in Escherichia coli Clostridium acetobutylicum

Protein Variants

Protein Variants Comment Organism
DELTAkdpX truncation of the kdpX gene leads to a less efficient K+-pump than wild-type Clostridium acetobutylicum
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
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
DELTAkdpZY loss of K+ transport Clostridium acetobutylicum

Organism

Organism UniProt Comment Textmining
Clostridium acetobutylicum
-
-
-

Specific Activity [micromol/min/mg]

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