3.4.24.B26: myroilysin
This is an abbreviated version!
For detailed information about myroilysin, go to the full flat file.
Word Map on EC 3.4.24.B26
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3.4.24.B26
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myroides
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metalloproteases
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profundi
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deep-sea
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astacin
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medicine
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synthesis
- 3.4.24.B26
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myroides
- metalloproteases
- profundi
-
deep-sea
- astacin
- medicine
- synthesis
Reaction
broad specificity, elastinolytic activity and collagen-swelling ability =
Synonyms
M10.064, More, MPR_2201
ECTree
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Substrates Products on EC 3.4.24.B26 - myroilysin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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?
Fibrin + H2O
?
hydrolyzes alpha, beta and gamma fibrin. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin
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?
N-succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + p-nitroaniline
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-
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?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
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?
N-succinyl-Phe-Ala-Ala-Phe-p-nitroanilide + H2O
N-succinyl-Phe-Ala-Ala-Phe + p-nitroaniline
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?
bovine elastin + H2O
?
myroilysin preferentially cleaves peptide bonds of bovine elastin with hydrophobic residues at the P1' and/or P1 positions
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?
bovine elastin + H2O
?
myroilysin preferentially cleaves peptide bonds of bovine elastin with hydrophobic residues at the P1' and/or P1 positions
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?
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
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?
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
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?
Fibrinogen + H2O
?
hydrolyzes Aalpha and Bbeta fibrinogen. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin
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?
Fibrinogen + H2O
?
hydrolyzes Aalpha and Bbeta fibrinogen. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin
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?
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
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?
Insulin B-chain + H2O
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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
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?
additional information
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myroilysin has broad specificity, no activity with: furylacryloyl-Gly-Leu-NH2, furylacryloyl-Gly-Phe-NH2
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?
additional information
?
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myroilysin has broad specificity, no activity with: furylacryloyl-Gly-Leu-NH2, furylacryloyl-Gly-Phe-NH2
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?
additional information
?
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myroilysin has broad specificity, no activity with: furylacryloyl-Gly-Leu-NH2, furylacryloyl-Gly-Phe-NH2
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?
