Literature summary for 3.4.24.B26 extracted from

Xu, D.; Zhou, J.; Lou, X.; He, J.; Ran, T.; Wang, W.
Myroilysin is a new bacterial member of the M12A family of metzincin metallopeptidases and is activated by a cysteine switch mechanism (2017), J. Biol. Chem., 292, 5195-5206 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of pro-myroilysin. The catalytic zinc ion of pro-myroilysin, at the bottom of a deep active site, is coordinated by three histidine residues in the conserved motif HEXXHXXGXXH. The cysteine residue in the propeptide coordinates the catalytic zinc ion and inhibits myroilysin activity. A cap structure tops the active site cleft in the structure of pro-myroilysin	Myroides profundi

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zinc	the catalytic zinc ion of pro-myroilysin, at the bottom of a deep active site, is coordinated by three histidine residues in the conserved motif HEXXHXXGXXH	Myroides profundi

Organism

Organism	UniProt	Comment	Textmining
Myroides profundi	B5B0E6	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	enzyme is synthesized as an inactive precursor	Myroides profundi

Synonyms

Synonyms	Comment	Organism
MPR_2201	-	Myroides profundi

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Release 2023.1 (January 2023)