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Literature summary for 3.1.1.61 extracted from

  • Anand, G.S.; Stock, A.M.
    Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB (2002), Biochemistry, 41, 6752-6760.
    View publication on PubMed
Search for more literature for 3.1.1.61

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Salmonella enterica subsp. enterica serovar Typhimurium
expression in Escherichia coli Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
additional information constructs of the N- and C-terminal domains and investigation of interaction between the isolated regulatory and effector domains of enzyme Salmonella enterica subsp. enterica serovar Typhimurium
additional information constructs of the N- and C-terminal domains and investigation of interaction between the isolated regulatory and effector domains of enzyme Thermotoga maritima

Inhibitors

Inhibitors Comment Organism Structure
additional information the unphosphorylated regulator domain partially inhibits methylesterase Salmonella enterica subsp. enterica serovar Typhimurium
additional information the unphosphorylated regulator domain partially inhibits methylesterase Thermotoga maritima
P2 domain of histidine kinase inhibition is decreased upon phosphorylation Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
Thermotoga maritima
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein In its unphosphorylated state, the regulatory domain inhibits enzyme activity of effector domain. Phosphorylation of the regulator domain leads to an enhancement of enzyme activity through a relief of inhibition and a stimulatory effect on catalysis. Salmonella enterica subsp. enterica serovar Typhimurium
phosphoprotein In its unphosphorylated state, the regulatory domain inhibits enzyme activity of effector domain. Phosphorylation of the regulator domain leads to an enhancement of enzyme activity through a relief of inhibition and a stimulatory effect on catalysis. Thermotoga maritima

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Salmonella enterica subsp. enterica serovar Typhimurium
recombinant enzyme Thermotoga maritima

Reaction

Reaction Comment Organism Reaction ID
protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol the enzyme is a response regulator protein in the bacterial chemotaxis two-component signal transduction pathway Salmonella enterica subsp. enterica serovar Typhimurium
a

Subunits

Subunits Comment Organism
More the CheB protein is composed of at least 2 structurally distinct proportions: a C-terminal catalytic domain, and a N-terminal region which modulates esterase activity Salmonella enterica subsp. enterica serovar Typhimurium
More the CheB protein is composed of at least 2 structurally distinct proportions: a C-terminal catalytic domain, and a N-terminal region which modulates esterase activity Thermotoga maritima

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0025
-
 P2 domain of histidine kinase pH 7.0, 25°C, in absence of phosphoramidate Salmonella enterica subsp. enterica serovar Typhimurium
0.021
-
 P2 domain of histidine kinase pH 7.0, 25°C, in presence of phosphoramidate Salmonella enterica subsp. enterica serovar Typhimurium