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

BRENDA support

Literature summary for 3.1.1.61 extracted from

  • Saxl, R.L.; Anand, G.S.; Stock, A.M.
    Synthesis and Biochemical Characterization of a Phosphorylated Analogue of the Response Regulator CheB (2001), Biochemistry, 40, 12896-12903.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C207S/C309S wild-type and mutant enzyme show significantly greater activity than the unphosphorylated proteins Salmonella enterica subsp. enterica serovar Typhimurium
D56C/C207S/C309S the half-life of mutant-SPO3 is 28 days, the unphosphorylated wild-type and mutant enzyme show the same enzyme activities Salmonella enterica subsp. enterica serovar Typhimurium

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein enzyme is activated in vivo by phosphorylation of a single aspartate, Asp56, in its regulatory domain Salmonella enterica subsp. enterica serovar Typhimurium

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

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