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Literature summary for 2.7.8.28 extracted from
- Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F(420) biosynthesis in Methanococcus jannaschii (2002), Biochemistry, 41, 3754-3761.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Methanocaldococcus jannaschii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S211A | mutant enzyme has the same specific activity as the wild type enzyme | Methanocaldococcus jannaschii |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Methanocaldococcus jannaschii |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.017 | - |
lactyl-2-diphospho-5'-guanosine | pH 7.0, 37°C | Methanocaldococcus jannaschii | |
| 0.032 | - |
7,8-didemethyl-8-hydroxy-5-deazariboflavin | pH 7.0, 37°C | Methanocaldococcus jannaschii | |
| 0.515 | - |
lactyl-2-diphospho-5'-adenosine | pH 7.0, 37°C | Methanocaldococcus jannaschii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | isolated CofD enzyme is not activated by the addition of 0-4 mM MgCl2. The inactivation by EDTA can be completely reversed by the addition of excess Mg2+ but not by the addition of Zn2+ or Mn2+ | Methanocaldococcus jannaschii | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 34400 | - |
2 * 34400, SDS-PAGE | Methanocaldococcus jannaschii |
| 66700 | - |
gel filtration | Methanocaldococcus jannaschii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin | Methanocaldococcus jannaschii | the reaction is the fourth step in the biosynthesis of coenzyme F420 | guanosine 5'-phosphate + coenzyme F420-0 | coenzyme F420-0 is coenzyme F420 without glutamic acid | ? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanocaldococcus jannaschii | Q58653 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Methanocaldococcus jannaschii |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| (2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + coenzyme F420-0 | coenzyme F420-0 is coenzyme F420 without glutamic acid | Methanocaldococcus jannaschii |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.36 | - |
- |
Methanocaldococcus jannaschii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lactyl-2-diphospho-5'-adenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin | catalysis does not appear to proceed via a covalent intermediate | Methanocaldococcus jannaschii | adenosine 5'-phosphate + coenzyme F420-0 | coenzyme F420-0 is coenzyme F420 without glutamic acid | ? | |
| lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin | the reaction is the fourth step in the biosynthesis of coenzyme F420 | Methanocaldococcus jannaschii | guanosine 5'-phosphate + coenzyme F420-0 | coenzyme F420-0 is coenzyme F420 without glutamic acid | ? | |
| lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin | catalysis does not appear to proceed via a covalent intermediate. Lactyl-2-diphospho-5'-guanosine is the preferred substrate. The substrate binding site of CofD is very specific for 7,8-didemethyl-8-hydroxy-5-deazariboflavin | Methanocaldococcus jannaschii | guanosine 5'-phosphate + coenzyme F420-0 | coenzyme F420-0 is coenzyme F420 without glutamic acid | ? | |
| additional information | to a lesser extent CofD also catalyzes a number of additional reactions that include the formation of 7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate, when the enzyme is incubated with 7,8-didemethyl-8-hydroxy-5-deazariboflavin and GDP, GTP, diphosphate, or tripolyphosphate, and the hydrolysis of F420-0 (F420 without glutamic acids) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin | Methanocaldococcus jannaschii | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 34400, SDS-PAGE | Methanocaldococcus jannaschii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2-phospho-L-lactate transferase | - |
Methanocaldococcus jannaschii |
| CofD | - |
Methanocaldococcus jannaschii |
| lactyl-2-diphospho-(5')guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase | - |
Methanocaldococcus jannaschii |
| lactyl-2-diphospho-(5')guanosine:Fo 2-phospho-L-lactate transferase | - |
Methanocaldococcus jannaschii |
| LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase | - |
Methanocaldococcus jannaschii |
| LPPG:Fo 2-phospho-L-lactate transferase | - |
Methanocaldococcus jannaschii |
| MJ1256 | - |
Methanocaldococcus jannaschii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Methanocaldococcus jannaschii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
24 h, completely stable | Methanocaldococcus jannaschii |
| 110 | - |
30 min, complete inactivation | Methanocaldococcus jannaschii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Methanocaldococcus jannaschii |
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