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Information on EC 4.3.99.4 - choline trimethylamine-lyase and Organism(s) Oleidesulfovibrio alaskensis and UniProt Accession Q30W70
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4.3.99.4 choline trimethylamine-lyaseIUBMB Comments
The enzyme utilizes a glycine radical to break the C-N bond in choline. Found in choline-degrading anaerobic bacteria.
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Word Map
- 4.3.99.4
- toluene
- p-cresol
- formate-lyase
-
thiyl
- 4-hydroxyphenylacetate
- aromatica
- thauera
-
r-benzylsuccinate
-
radical-based
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
glycyl radical enzyme, choline tma-lyase, choline trimethylamine-lyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
choline = trimethylamine + acetaldehyde
radical reaction or rearrangement mechanism, overview
Oleidesulfovibrio alaskensis
-
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.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Oleidesulfovibrio alaskensis
-
the enzyme CutC is a C-N bond-cleaving glycyl radical enzyme
-
-
?
choline
trimethylamine + acetaldehyde
Oleidesulfovibrio alaskensis
-
a glycyl radical-based mechanism of C-N cleavage
-
?
choline
trimethylamine + acetaldehyde
Oleidesulfovibrio alaskensis
important route for the production of trimethylamine
-
-
?
choline
trimethylamine + acetaldehyde
Oleidesulfovibrio alaskensis
-
the enzyme shows strict specificity for choline
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
choline
trimethylamine + acetaldehyde
Oleidesulfovibrio alaskensis
important route for the production of trimethylamine
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GRE activating protein
Oleidesulfovibrio alaskensis
-
i.e. CutD, biochemical function of CutD as a glycyl radical enzyme or CutC activase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3025
choline
Oleidesulfovibrio alaskensis
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
747
choline
Oleidesulfovibrio 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
LITERATURE
22.7
Oleidesulfovibrio alaskensis
-
purified recombinant enzyme, pH 8.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Oleidesulfovibrio alaskensis
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Oleidesulfovibrio alaskensis
gene disruption impairs growth on choline and abolishes production of trimethylamine, with no difference in growth between wild-type and mutant in media containing lactate. Expression of choline trimethylamine-lyase CutC and its activating protein CutD in Escherichia coli BL21 results in production of d9-TMA from (trimethyl-d9)-choline. Expression of either enzyme on its own completely abolishes trimethylamine production
evolution
Oleidesulfovibrio alaskensis
-
choline TMA-lyase belongs to the glycyl radical enzymes (GREs) utilize protein-based radical intermediates to catalyze a variety of reactions, including nucleotide reduction (class III ribonucleotide reductase (RNR)), C-C bond formation (benzylsuccinate synthase (BSS)), C-C bond cleavage (pyruvate formate-lyase (PFL) and 4-hydroxyphenylacetate decarboxylase (4-HPAD)), and dehydration (B12-independent glycerol dehydratase (GDH))
metabolism
Oleidesulfovibrio alaskensis
-
the enzyme is involved in anaerobic choline metabolism and encoded in the choline utilization (cut) gene cluster
additional information
Oleidesulfovibrio alaskensis
-
enzyme homology modeling, docking of choline in the active site of a the enzyme, docking model, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
Oleidesulfovibrio alaskensis
-
dimeric oligomerization state for full-length CutC and all of the variants
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T502A
Oleidesulfovibrio alaskensis
turnover number for choline is 4400fold lower than for wild-type enzyme
Y208F
Oleidesulfovibrio alaskensis
turnover number for choline is 215fold lower than for wild-type enzyme
Y208F/Y506F
Oleidesulfovibrio alaskensis
turnover number for choline is 1050fold lower than for wild-type enzyme
Y506F
Oleidesulfovibrio alaskensis
turnover number for choline is 48fold lower than for wild-type enzyme
additional information
Oleidesulfovibrio alaskensis
-
condtruction of a -52 amino acid truncated variant, removal of the predicted N-terminal microcompartment targeting sequence from CutC improves yields and solubility without impacting activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged wild-type and point and N-terminal truncation mutant enzymes from Escherichia coli
Oleidesulfovibrio alaskensis
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cutC, cloning and overexpression of the N-terminally His6-tagged wild-type and point and N-terminal truncation mutant enzymes in Escherichia coli
Oleidesulfovibrio alaskensis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Craciun, S.; Balskus, E.P.
Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme
Proc. Natl. Acad. Sci. USA
109
21307-21312
2012
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans (B8J0I2), Oleidesulfovibrio alaskensis (Q30W70), Oleidesulfovibrio alaskensis G20 (Q30W70)
Craciun, S.; Marks, J.A.; Balskus, E.P.
Characterization of choline trimethylamine-lyase expands the chemistry of glycyl radical enzymes
ACS Chem. Biol.
9
1408-1413
2014
Oleidesulfovibrio alaskensis, Oleidesulfovibrio alaskensis G20
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Release 2023.1 (January 2023)
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