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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.1.61 - protein-glutamate methylesterase and Organism(s) Escherichia coli and UniProt Accession P07330

for references in articles please use BRENDA:EC3.1.1.61
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.61 protein-glutamate methylesterase
IUBMB Comments
Hydrolyses the products of EC 2.1.1.77 (protein-L-isoaspartate(D-aspartate) O-methyltransferase), EC 2.1.1.78 (isoorientin 3'-O-methyltransferase), EC 2.1.1.80 (protein-glutamate O-methyltransferase) and EC 2.1.1.100 (protein-S-isoprenylcysteine O-methyltransferase).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P07330
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
  • 3.1.1.61
  • chemotactic
  • chemoreceptor
  • chey
  • tumbling
  • chemotaxis-like
  • methylation-demethylation
  • mcp-like
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
methyl-accepting chemotaxis protein, protein methylesterase, methylesterase cheb, cheb methylesterase, chemotaxis-specific methylesterase, chemotaxis receptor mcpb, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CheB methylesterase
-
-
-
-
chemotaxis-specific methylesterase
-
-
-
-
esterase, methyl-accepting chemotaxis protein methyl-
-
-
-
-
esterase, protein methyl-
-
-
-
-
methyl-accepting chemotaxis protein
-
-
-
-
methylesterase CheB
PME
-
-
-
-
protein carboxyl methylesterase
-
-
-
-
protein methylesterase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-L-glutamate-O5-methyl-ester acylhydrolase
Hydrolyses the products of EC 2.1.1.77 (protein-L-isoaspartate(D-aspartate) O-methyltransferase), EC 2.1.1.78 (isoorientin 3'-O-methyltransferase), EC 2.1.1.80 (protein-glutamate O-methyltransferase) and EC 2.1.1.100 (protein-S-isoprenylcysteine O-methyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
69552-31-4
-
93792-01-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
CheB localizes to a cell pole in presence of the chemoreceptor MCP, binding of the NL domain to the P2 domain targets methylesterase CheB to the polar signalling complex
-
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
the regulation of activity of methylesterase CheB via phosphorylation is central to chemotactic adaption
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C207A
-
mutant retains at least 50% of the wild-type enzyme activity
C207A/C309A
-
the double mutant retains at 70% of the wild-type enzyme activity
C309A
-
mutant retains at least 50% of the wild-type enzyme activity
S164C
-
mutant has less than 2% of the wild-type activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kehry, M.R.; Doak, T.G.; Dahlquist, F.W.
Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli
J. Biol. Chem.
259
11828-11835
1984
Escherichia coli
Manually annotated by BRENDA team
Krueger, J.K.; Stock, J.; Schutt, C.E.
Evidence that the methylesterase of bacterial chemotaxis may be a serine hydrolase
Biochim. Biophys. Acta
1119
322-326
1992
Escherichia coli, Escherichia coli JM 109
Manually annotated by BRENDA team
Lybarger, S.R.; Maddock, J.R.
Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB
J. Bacteriol.
181
5527-5529
1999
Escherichia coli
Manually annotated by BRENDA team
Barnakov, A.N.; Barnakova, L.A.; Hazelbauer, G.L.
Location of the receptor-interaction site on CheB, the methylesterase response regulator of bacterial chemotaxis
J. Biol. Chem.
276
32984-32989
2001
Escherichia coli
Manually annotated by BRENDA team
Banno, S.; Shiomi, D.; Homma, M.; Kawagishi, I.
Targeting of the chemotaxis methylesterase/deamidase CheB to the polar receptor-kinase cluster in an Escherichia coli cell
Mol. Microbiol.
53
1051-1063
2004
Escherichia coli
Manually annotated by BRENDA team
Li, M.; Hazelbauer, G.L.
The carboxyl-terminal linker is important for chemoreceptor function
Mol. Microbiol.
60
469-479
2006
Escherichia coli
Manually annotated by BRENDA team
Endres, R.G.; Wingreen, N.S.
Precise adaptation in bacterial chemotaxis through assistance neighborhoods
Proc. Natl. Acad. Sci. USA
103
13040-13044
2006
Escherichia coli (P07330)
Manually annotated by BRENDA team