Information on EC 4.3.99.4 - choline trimethylamine-lyase

Word Map on EC 4.3.99.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Desulfovibrio

EC NUMBER
COMMENTARY hide
4.3.99.4
-
RECOMMENDED NAME
GeneOntology No.
choline trimethylamine-lyase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
choline = trimethylamine + acetaldehyde
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
choline degradation III
-
-
phosphatidylethanolamine bioynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
choline trimethylamine-lyase (acetaldehyde-forming)
The enzyme utilizes a glycine radical to break the C-N bond in choline. Found in choline-degrading anaerobic bacteria.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
member of the glycyl radical enzyme family
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
choline
trimethylamine + acetaldehyde
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
choline
trimethylamine + acetaldehyde
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GRE activating protein
-
i.e. CutD, biochemical function of CutD as a glycyl radical enzyme or CutC activase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3025
choline
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
747
choline
Desulfovibrio alaskensis
-
calculated from the EPR activation measurement, recombinant enzyme, pH 8.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22.7
-
purified recombinant enzyme, pH 8.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Desulfovibrio alaskensis (strain G20)
Desulfovibrio alaskensis (strain G20)
Desulfovibrio alaskensis (strain G20)
Desulfovibrio alaskensis (strain G20)
Desulfovibrio alaskensis (strain G20)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged wild-type and point and N-terminal truncation mutant enzymes from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene cutC, cloning and overexpression of the N-terminally His6-tagged wild-type and point and N-terminal truncation mutant enzymes in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C489A
complete loss of activity
G821A
complete loss of activity
T334S
-
site-directed mutagenesis, the mutant retains activity
T502S
-
site-directed mutagenesis, the mutant retains activity
C489A
-
complete loss of activity
-
G821A
-
complete loss of activity
-
T334S
-
site-directed mutagenesis, the mutant retains activity
-
T502S
-
site-directed mutagenesis, the mutant retains activity
-
additional information
Show AA Sequence (294 entries)
Please use the Sequence Search for a specific query.