Any feedback?
Literature summary for 4.3.99.4 extracted from
- Characterization of choline trimethylamine-lyase expands the chemistry of glycyl radical enzymes (2014), ACS Chem. Biol., 9, 1408-1413.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| GRE activating protein | i.e. CutD, biochemical function of CutD as a glycyl radical enzyme or CutC activase | Oleidesulfovibrio alaskensis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| T334S | site-directed mutagenesis, the mutant retains activity | Oleidesulfovibrio alaskensis |
| T502S | site-directed mutagenesis, the mutant retains activity | Oleidesulfovibrio alaskensis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.3025 | - |
choline | recombinant enzyme, pH 8.0, temperature not specified in the publication | Oleidesulfovibrio alaskensis |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| choline | Oleidesulfovibrio alaskensis | - |
trimethylamine + acetaldehyde | - |
? | |
| choline | Oleidesulfovibrio alaskensis G20 | - |
trimethylamine + acetaldehyde | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oleidesulfovibrio alaskensis | - |
gene cutC | - |
| Oleidesulfovibrio alaskensis G20 | - |
gene cutC | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His6-tagged wild-type and point and N-terminal truncation mutant enzymes from Escherichia coli | Oleidesulfovibrio alaskensis |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| choline = trimethylamine + acetaldehyde | radical reaction or rearrangement mechanism, overview | Oleidesulfovibrio alaskensis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 22.7 | - |
purified recombinant enzyme, pH 8.0, temperature not specified in the publication | Oleidesulfovibrio alaskensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| choline | - |
Oleidesulfovibrio alaskensis | trimethylamine + acetaldehyde | - |
? | |
| choline | the enzyme shows strict specificity for choline | Oleidesulfovibrio alaskensis | trimethylamine + acetaldehyde | - |
? | |
| choline | - |
Oleidesulfovibrio alaskensis G20 | trimethylamine + acetaldehyde | - |
? | |
| choline | the enzyme shows strict specificity for choline | Oleidesulfovibrio alaskensis G20 | trimethylamine + acetaldehyde | - |
? | |
| additional information | the enzyme CutC is a C-N bond-cleaving glycyl radical enzyme | Oleidesulfovibrio alaskensis | ? | - |
? | |
| additional information | the enzyme CutC is a C-N bond-cleaving glycyl radical enzyme | Oleidesulfovibrio alaskensis G20 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | dimeric oligomerization state for full-length CutC and all of the variants | Oleidesulfovibrio alaskensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| choline TMA-lyase | - |
Oleidesulfovibrio alaskensis |
| cutC | - |
Oleidesulfovibrio alaskensis |
| glycyl radical enzyme | - |
Oleidesulfovibrio alaskensis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 747 | - |
choline | calculated from the EPR activation measurement, recombinant enzyme, pH 8.0, temperature not specified in the publication | Oleidesulfovibrio alaskensis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Oleidesulfovibrio alaskensis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| metabolism | the enzyme is involved in anaerobic choline metabolism and encoded in the choline utilization (cut) gene cluster | Oleidesulfovibrio alaskensis |
| additional information | enzyme homology modeling, docking of choline in the active site of a the enzyme, docking model, overview | Oleidesulfovibrio alaskensis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
