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Literature summary for 3.4.24.B26 extracted from
- Ecological function of myroilysin, a novel bacterial M12 metalloprotease with elastinolytic activity and a synergistic role in collagen hydrolysis, in biodegradation of deep-sea high-molecular-weight organic nitrogen (2009), Appl. Environ. Microbiol., 75, 1838-1844.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Myroides profundi |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1,10-phenanthroline | 4 mM, complete inhibition | Myroides profundi |  |
| Co2+ | inhibits the caseinolytic and elastinolytic activities | Myroides profundi | |
| EDTA | moderate inhibitory effect | Myroides profundi | |
| EGTA | moderate inhibitory effect | Myroides profundi | |
| Fe2+ | inhibits the caseinolytic and elastinolytic activities | Myroides profundi | |
| additional information | Li+, K+, Mg2+, Ca2+, Sr2+, Ba2+, and Na+ have a little or no effect on activity | Myroides profundi | |
| Ni2+ | inhibits the caseinolytic and elastinolytic activities | Myroides profundi | |
| Sr2+ | inhibits the caseinolytic and elastinolytic activities | Myroides profundi | |
| Zn2+ | inhibits the caseinolytic and elastinolytic activities | Myroides profundi | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km-value for casein at 50°C is 0.38% | Myroides profundi |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn | the enzyme has the same conserved residues at the four zinc ligands as astacin (EC 3.4.24.21) | Myroides profundi | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 22936 | - |
1 * 22936, mass spectrometry | Myroides profundi |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Collagen + H2O | Myroides profundi | insoluble type I collagen fibre. Although it displays very low activity with collagen, myroilysin has strong collagen-swelling ability and plays a synergistic role with collagenase in collagen hydrolysis | ? | - |
? | |
| Collagen + H2O | Myroides profundi D25 | insoluble type I collagen fibre. Although it displays very low activity with collagen, myroilysin has strong collagen-swelling ability and plays a synergistic role with collagenase in collagen hydrolysis | ? | - |
? | |
| Elastin + H2O | Myroides profundi | the enzyme shows much higher elastinolytic activity than the bacterial elastinase pseudolysin (EC 3.4.24.26). It has 6.78 U/mg elastinolytic activity in artificial seawater at 4°C, suggesting that it probably can degrade elastin in the deep sea | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Myroides profundi | B5B0E6 | - |
- |
| Myroides profundi D25 | B5B0E6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Myroides profundi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | - |
Myroides profundi | ? | - |
? | |
| casein + H2O | - |
Myroides profundi D25 | ? | - |
? | |
| Collagen + H2O | insoluble type I collagen fibre. Although it displays very low activity with collagen, myroilysin has strong collagen-swelling ability and plays a synergistic role with collagenase in collagen hydrolysis | Myroides profundi | ? | - |
? | |
| Collagen + H2O | insoluble type I collagen fibre. Although it displays very low activity with collagen, myroilysin has strong collagen-swelling ability and plays a synergistic role with collagenase in collagen hydrolysis | Myroides profundi D25 | ? | - |
? | |
| Elastin + H2O | the enzyme shows much higher elastinolytic activity than the bacterial elastinase pseudolysin (EC 3.4.24.26). It has 6.78 U/mg elastinolytic activity in artificial seawater at 4°C, suggesting that it probably can degrade elastin in the deep sea | Myroides profundi | ? | - |
? | |
| elastinorcein + H2O | - |
Myroides profundi | ? | - |
? | |
| Fibrin + H2O | hydrolyzes alpha, beta and gamma fibrin. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin | Myroides profundi | ? | - |
? | |
| Fibrinogen + H2O | hydrolyzes Aalpha and Bbeta fibrinogen. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin | Myroides profundi | ? | - |
? | |
| Fibrinogen + H2O | hydrolyzes Aalpha and Bbeta fibrinogen. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin | Myroides profundi D25 | ? | - |
? | |
| Gelatin + H2O | - |
Myroides profundi | ? | - |
? | |
| Insulin B-chain + H2O | the T27-P28 peptide bond is the most susceptible cleavage site, and the highest hydrolytic rate is observed for this bond. The hydrolytic rates for peptide bonds S9-H10, H10-L11, F25-Y26, and Y26-T27 are also comparatively high, and the hydrolytic rates for peptide bonds N3-Q4, H5-L6, L6-C7, Y16-L17, and K29-A30 are comparatively low | Myroides profundi | ? | - |
? | |
| Insulin B-chain + H2O | the T27-P28 peptide bond is the most susceptible cleavage site, and the highest hydrolytic rate is observed for this bond. The hydrolytic rates for peptide bonds S9-H10, H10-L11, F25-Y26, and Y26-T27 are also comparatively high, and the hydrolytic rates for peptide bonds N3-Q4, H5-L6, L6-C7, Y16-L17, and K29-A30 are comparatively low | Myroides profundi D25 | ? | - |
? | |
| additional information | myroilysin has broad specificity, no activity with: furylacryloyl-Gly-Leu-NH2, furylacryloyl-Gly-Phe-NH2 | Myroides profundi | ? | - |
? | |
| additional information | myroilysin has broad specificity, no activity with: furylacryloyl-Gly-Leu-NH2, furylacryloyl-Gly-Phe-NH2 | Myroides profundi D25 | ? | - |
? | |
| N-succinyl-Ala-Ala-Ala-p-nitroanilide + H2O | - |
Myroides profundi | N-succinyl-Ala-Ala-Ala + p-nitroaniline | - |
? | |
| N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O | - |
Myroides profundi | N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline | - |
? | |
| N-succinyl-Phe-Ala-Ala-Phe-p-nitroanilide + H2O | - |
Myroides profundi | N-succinyl-Phe-Ala-Ala-Phe + p-nitroaniline | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 22936, mass spectrometry | Myroides profundi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| M10.064 | Merops ID | Myroides profundi |
| More | metalloprotease belonging to subfamily M12A | Myroides profundi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 45 | pH 9.0, substrate: elastinorcein | Myroides profundi |
| 50 | - |
pH 9.0, substrate: casein | Myroides profundi |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
half-life: 28 min | Myroides profundi |
| 43 | - |
apparent melting temperature is 42.6°C | Myroides profundi |
| 45 | - |
half-life: 5 min | Myroides profundi |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
at 40°C, substrate: elastinorcein | Myroides profundi |
| 9.5 | - |
at 50°C; substrate: casein | Myroides profundi |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Myroides profundi | calculated from sequence | - |
6.3 |
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