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

BRENDA support

Literature summary extracted from

  • Schmees, G.; Stein, A.; Hunke, S.; Landmesser, H.; Schneider, E.
    Functional consequences of mutation in the conserved signature sequence of the ATP-binding-cassette protein MalK (1999), Eur. J. Biochem., 266, 420-430.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
7.5.2.1 G137A mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 G137T mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 G137V mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 Q140K mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, ATPase activity and MgATP-induced changes in tryptic cleavage pattern similar to those of wild-type. Mutant transport complexes containing MalKQ140K variant, when studied in proteoliposomes, are severely impaired in MalE-maltose-stimulated ATPase activity Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 Q140L mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, fails to hydrolyze ATP and exhibits a strong intrinsic resistance to trypsin in the absence of MgATP, suggesting a drastically altered conformation Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 Q140N mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, ATPase activity and MgATP-induced changes in tryptic cleavage pattern similar to those of wild-type. Mutant transport complexes containing MalKQ140N variant, when studied in proteoliposomes, are severely impaired in MalE-maltose-stimulated ATPase activity Salmonella enterica subsp. enterica serovar Typhimurium

General Stability

EC Number General Stability Organism
7.5.2.1 MgATP2-, binding protects against trypsin inactivation in wild-type enzyme in in G137 mutants Salmonella enterica subsp. enterica serovar Typhimurium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
7.5.2.1 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.5.2.1 ATP + H2O + maltose/out
-
Salmonella enterica subsp. enterica serovar Typhimurium ADP + phosphate + maltose/in
-
?