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Literature summary extracted from

  • Chen, X.L.; Xie, B.B.; Bian, F.; Zhao, G.Y.; Zhao, H.L.; He, H.L.; Zhou, B.C.; Zhang, Y.Z.
    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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B26
-
 Myroides profundi

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B26 1,10-phenanthroline 4 mM, complete inhibition Myroides profundi
3.4.24.B26 Co2+ inhibits the caseinolytic and elastinolytic activities Myroides profundi
3.4.24.B26 EDTA moderate inhibitory effect Myroides profundi
3.4.24.B26 EGTA moderate inhibitory effect Myroides profundi
3.4.24.B26 Fe2+ inhibits the caseinolytic and elastinolytic activities Myroides profundi
3.4.24.B26 additional information Li+, K+, Mg2+, Ca2+, Sr2+, Ba2+, and Na+ have a little or no effect on activity Myroides profundi
3.4.24.B26 Ni2+ inhibits the caseinolytic and elastinolytic activities Myroides profundi
3.4.24.B26 Sr2+ inhibits the caseinolytic and elastinolytic activities Myroides profundi
3.4.24.B26 Zn2+ inhibits the caseinolytic and elastinolytic activities Myroides profundi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.24.B26 additional information
-
 additional information Km-value for casein at 50°C is 0.38% Myroides profundi

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B26 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.B26 22936
-
 1 * 22936, mass spectrometry Myroides profundi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.B26 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 ?
-
 ?
3.4.24.B26 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 ?
-
 ?
3.4.24.B26 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

EC Number Organism UniProt Comment Textmining
3.4.24.B26 Myroides profundi B5B0E6
-
-
3.4.24.B26 Myroides profundi D25 B5B0E6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.B26
-
 Myroides profundi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B26 casein + H2O
-
 Myroides profundi ?
-
 ?
3.4.24.B26 casein + H2O
-
 Myroides profundi D25 ?
-
 ?
3.4.24.B26 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 ?
-
 ?
3.4.24.B26 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 ?
-
 ?
3.4.24.B26 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 ?
-
 ?
3.4.24.B26 elastinorcein + H2O
-
 Myroides profundi ?
-
 ?
3.4.24.B26 Fibrin + H2O hydrolyzes alpha, beta and gamma fibrin. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin Myroides profundi ?
-
 ?
3.4.24.B26 Fibrinogen + H2O hydrolyzes Aalpha and Bbeta fibrinogen. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin Myroides profundi ?
-
 ?
3.4.24.B26 Fibrinogen + H2O hydrolyzes Aalpha and Bbeta fibrinogen. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin Myroides profundi D25 ?
-
 ?
3.4.24.B26 Gelatin + H2O
-
 Myroides profundi ?
-
 ?
3.4.24.B26 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 ?
-
 ?
3.4.24.B26 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 ?
-
 ?
3.4.24.B26 additional information myroilysin has broad specificity, no activity with: furylacryloyl-Gly-Leu-NH2, furylacryloyl-Gly-Phe-NH2 Myroides profundi ?
-
 ?
3.4.24.B26 additional information myroilysin has broad specificity, no activity with: furylacryloyl-Gly-Leu-NH2, furylacryloyl-Gly-Phe-NH2 Myroides profundi D25 ?
-
 ?
3.4.24.B26 N-succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
-
 Myroides profundi N-succinyl-Ala-Ala-Ala + p-nitroaniline
-
 ?
3.4.24.B26 N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
-
 Myroides profundi N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
 ?
3.4.24.B26 N-succinyl-Phe-Ala-Ala-Phe-p-nitroanilide + H2O
-
 Myroides profundi N-succinyl-Phe-Ala-Ala-Phe + p-nitroaniline
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B26 monomer 1 * 22936, mass spectrometry Myroides profundi

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B26 M10.064 Merops ID Myroides profundi
3.4.24.B26 More metalloprotease belonging to subfamily M12A Myroides profundi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.B26 40 45 pH 9.0, substrate: elastinorcein Myroides profundi
3.4.24.B26 50
-
 pH 9.0, substrate: casein Myroides profundi

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.B26 40
-
 half-life: 28 min Myroides profundi
3.4.24.B26 43
-
 apparent melting temperature is 42.6°C Myroides profundi
3.4.24.B26 45
-
 half-life: 5 min Myroides profundi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.B26 9
-
 at 40°C, substrate: elastinorcein Myroides profundi
3.4.24.B26 9.5
-
 at 50°C; substrate: casein Myroides profundi

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.24.B26 Myroides profundi calculated from sequence
-
 6.3