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Literature summary extracted from

  • Craciun, S.; Marks, J.A.; Balskus, E.P.
    Characterization of choline trimethylamine-lyase expands the chemistry of glycyl radical enzymes (2014), ACS Chem. Biol., 9, 1408-1413.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.3.99.4 GRE activating protein i.e. CutD, biochemical function of CutD as a glycyl radical enzyme or CutC activase Oleidesulfovibrio alaskensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.99.4 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

Protein Variants

EC Number Protein Variants Comment Organism
4.3.99.4 additional information 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 Oleidesulfovibrio alaskensis
4.3.99.4 T334S site-directed mutagenesis, the mutant retains activity Oleidesulfovibrio alaskensis
4.3.99.4 T502S site-directed mutagenesis, the mutant retains activity Oleidesulfovibrio alaskensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.99.4 0.3025
-
 choline recombinant enzyme, pH 8.0, temperature not specified in the publication Oleidesulfovibrio alaskensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.99.4 choline Oleidesulfovibrio alaskensis
-
 trimethylamine + acetaldehyde
-
 ?
4.3.99.4 choline Oleidesulfovibrio alaskensis G20
-
 trimethylamine + acetaldehyde
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.99.4 Oleidesulfovibrio alaskensis
-
 gene cutC
-
4.3.99.4 Oleidesulfovibrio alaskensis G20
-
 gene cutC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.99.4 recombinant N-terminally His6-tagged wild-type and point and N-terminal truncation mutant enzymes from Escherichia coli Oleidesulfovibrio alaskensis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.3.99.4 choline = trimethylamine + acetaldehyde radical reaction or rearrangement mechanism, overview Oleidesulfovibrio alaskensis
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.99.4 22.7
-
 purified recombinant enzyme, pH 8.0, temperature not specified in the publication Oleidesulfovibrio alaskensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.99.4 choline
-
 Oleidesulfovibrio alaskensis trimethylamine + acetaldehyde
-
 ?
4.3.99.4 choline the enzyme shows strict specificity for choline Oleidesulfovibrio alaskensis trimethylamine + acetaldehyde
-
 ?
4.3.99.4 choline
-
 Oleidesulfovibrio alaskensis G20 trimethylamine + acetaldehyde
-
 ?
4.3.99.4 choline the enzyme shows strict specificity for choline Oleidesulfovibrio alaskensis G20 trimethylamine + acetaldehyde
-
 ?
4.3.99.4 additional information the enzyme CutC is a C-N bond-cleaving glycyl radical enzyme Oleidesulfovibrio alaskensis ?
-
 ?
4.3.99.4 additional information the enzyme CutC is a C-N bond-cleaving glycyl radical enzyme Oleidesulfovibrio alaskensis G20 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.99.4 homodimer dimeric oligomerization state for full-length CutC and all of the variants Oleidesulfovibrio alaskensis

Synonyms

EC Number Synonyms Comment Organism
4.3.99.4 choline TMA-lyase
-
 Oleidesulfovibrio alaskensis
4.3.99.4 cutC
-
 Oleidesulfovibrio alaskensis
4.3.99.4 glycyl radical enzyme
-
 Oleidesulfovibrio alaskensis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.99.4 747
-
 choline calculated from the EPR activation measurement, recombinant enzyme, pH 8.0, temperature not specified in the publication Oleidesulfovibrio alaskensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.99.4 8
-
 assay at Oleidesulfovibrio alaskensis

General Information

EC Number General Information Comment Organism
4.3.99.4 evolution 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)) Oleidesulfovibrio alaskensis
4.3.99.4 metabolism the enzyme is involved in anaerobic choline metabolism and encoded in the choline utilization (cut) gene cluster Oleidesulfovibrio alaskensis
4.3.99.4 additional information enzyme homology modeling, docking of choline in the active site of a the enzyme, docking model, overview Oleidesulfovibrio alaskensis