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Literature summary for 7.5.2.1 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
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Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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

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

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
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Substrates and Products (Substrate)

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