Literature summary for 3.4.24.B26 extracted from

Yang, J.; Zhao, H.L.; Tang, B.L.; Chen, X.L.; Su, H.N.; Zhang, X.Y.; Song, X.Y.; Zhou, B.C.; Xie, B.B.; Weiss, A.S.; Zhang, Y.Z.
Mechanistic insight into the elastin degradation process by the metalloprotease myroilysin from the deep-sea bacterium Myroides profundi D25 (2015), Mar. Drugs, 13, 1481-1496.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Triton X-100	significantly decreases enzyme binding to elastin	Myroides profundi
Tween 20	significantly decreases enzyme binding to elastin	Myroides profundi
Tween 60	significantly decreases enzyme binding to elastin	Myroides profundi
Zn2+	-	Myroides profundi

Metals/Ions

Metals/Ions	Comment	Organism	Structure
NaCl	2 mM NaCl increases enzyme binding to the elastin fibres	Myroides profundi

Organism

Organism	UniProt	Comment	Textmining
Myroides profundi	B5B0E6	-	-
Myroides profundi D25	B5B0E6	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
bovine elastin + H2O	myroilysin preferentially cleaves peptide bonds of bovine elastin with hydrophobic residues at the P1' and/or P1 positions	Myroides profundi	?	-	?
bovine elastin + H2O	myroilysin preferentially cleaves peptide bonds of bovine elastin with hydrophobic residues at the P1' and/or P1 positions	Myroides profundi D25	?	-	?

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Release 2023.1 (January 2023)