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Literature summary for 4.4.1.31 extracted from
- Characterization of phycoviolobilin phycoerythrocyanin-alpha 84-cystein-lyase-(isomerizing) from Mastigocladus laminosus (2002), Eur. J. Biochem., 269, 4542-4550.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | 2-mercaptoethanol or thiols like such as dithiothreitol are required for the isomerization reaction of the lyase: without, only the phycocyanobilin addition product is formed, but no [phycoerythrocyanin alpha-subunit]-Cys84-phycoviolobilin. Too much 2-mercaptoethanol will cause the loss of chromophore, in a reaction requiring oxygen. When Mg2+ is used as the activator, the optimal concentration of 2-mercaptoethanol is 5 mM, with Mn2+ it is 3 mM | Mastigocladus laminosus |  |
| dithiothreitol | 2-mercaptoethanol or thiols like such as dithiothreitol are required for the isomerization reaction of the lyase: without, only the phycocyanobilin addition product is formed, but no [phycoerythrocyanin alpha-subunit]-Cys84-phycoviolobilin | Mastigocladus laminosus | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Mastigocladus laminosus |
General Stability
| General Stability | Organism |
|---|---|
| denaturation in 8 M urea of the individual subunits, PecE or PecF, is largely irreversible. If they are mixed together after dialysing out the urea separately, they show only little activity | Mastigocladus laminosus |
| repetitive freezing and thawing should be avoided, as it causes the purified proteins to precipitate | Mastigocladus laminosus |
| very stable preparations are obtained by adding an equal volume of glycerol before freezing | Mastigocladus laminosus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | 5 mM, complete inhibition | Mastigocladus laminosus | |
| Cu2+ | 5 mM, complete inhibition | Mastigocladus laminosus | |
| Fe2+ | 5 mM, complete inhibition | Mastigocladus laminosus | |
| Mg2+ | 25 mM, 38% inhibition | Mastigocladus laminosus | |
| Mn2+ | 25 mM, complete inhibition | Mastigocladus laminosus | |
| Ni2+ | 5 mM, complete inhibition | Mastigocladus laminosus | |
| potassium phosphate | the buffer decreases the effect of the activators, Mn2+ or Mg2+, by 20% as compared with Tris/HCl buffer | Mastigocladus laminosus | |
| Zn2+ | 5 mM, complete inhibition | Mastigocladus laminosus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0024 | - |
apo-[phycoerythrocyanin alpha-subunit] | at 0.014 mM (2R,3E)-phycocyanobilin, pH and temperature not specified in the publication | Mastigocladus laminosus | |
| 0.012 | 0.016 | (2R,3E)-phycocyanobilin | depending on apo-[phycoerythrocyanin alpha-subunit] (0.0048-0.019 mM), pH and temperature not specified in the publication | Mastigocladus laminosus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | less effective in activation (at 5 mM) than Mg2+ or Mn2+ | Mastigocladus laminosus | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+, optimum concentration of Mg2+ is 5 mM | Mastigocladus laminosus | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+, optimum concentration of Mn2+ is 3 mM | Mastigocladus laminosus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| apo-[phycoerythrocyanin alpha-subunit] + (2R,3E)-phycocyanobilin | Mastigocladus laminosus | the enzyme catalyses the covalent attachment of the phycobilin chromophore phycocyanobilin to cysteine 84 of the beta subunit of the phycobiliprotein phycoerythrocyanin and its isomerization to phycoviolobilin | [phycoerythrocyanin alpha-subunit]-Cys84-phycoviolobilin | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mastigocladus laminosus | P29729 and P29730 | P29729: bilin biosynthesis protein PecE, P29730: bilin biosynthesis protein PecF | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| His-tagged PecE and PecF | Mastigocladus laminosus |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C, 1 year, His-tagged PecE and PecF are stable | Mastigocladus laminosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| apo-[phycoerythrocyanin alpha-subunit] + (2R,3E)-phycocyanobilin | the enzyme catalyses the covalent attachment of the phycobilin chromophore phycocyanobilin to cysteine 84 of the beta subunit of the phycobiliprotein phycoerythrocyanin and its isomerization to phycoviolobilin | Mastigocladus laminosus | [phycoerythrocyanin alpha-subunit]-Cys84-phycoviolobilin | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | formation of complexes between the subunits, PecE and PecF | Mastigocladus laminosus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| phycoviolobilin phycoerythrocyanin-alpha84-cystein-lyase | - |
Mastigocladus laminosus |
| PVBPEC-lyase | - |
Mastigocladus laminosus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
room temperature is recommended in the absence of Triton X-100, because the proteins tend to precipitate at 37°C. In the presence of Triton X-100 (1% v/v) the temperature can be increased without precipitation to 37°C (Mg2+ as activator), or even to 45°C (Mn2+ as activator) | Mastigocladus laminosus |
| 37 | - |
room temperature is recommended in the absence of Triton X-100, because the proteins tend to precipitate at 37°C. In the presence of Triton X-100 (1% v/v) the temperature can be increased without precipitation to 37°C with Mg2+ as activator | Mastigocladus laminosus |
| 45 | - |
room temperature is recommended in the absence of Triton X-100, because the proteins tend to precipitate at 37°C. In the presence of Triton X-100 (1% v/v) the temperature can be increased without precipitation to 45°C with Mn2+ as activator | Mastigocladus laminosus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00001 | 0.00013 | apo-[phycoerythrocyanin alpha-subunit] | depending on apo phycoerythrocyanin alpha-subunit (0.0048-0.019 mM), pH and temperature not specified in the publication | Mastigocladus laminosus | |
| 0.000074 | - |
(2R,3E)-phycocyanobilin | at 0.014 mM apo phycoerythrocyanin alpha-subunit, pH and temperature not specified in the publication | Mastigocladus laminosus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 7.8 | - |
Mastigocladus laminosus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 8.5 | pH 7.0: about 40% of maximal activity, pH 8.5: about 60% of maximal activity | Mastigocladus laminosus |
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