Literature summary for 3.4.21.20 extracted from

Shao, B.; Belaaouaj, A.; Verlinde, C.L.; Fu, X.; Heinecke, J.W.
Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase (2005), J. Biol. Chem., 280, 29311-29321.

Search for more literature for 3.4.21.20

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	hypochlorous acid, a specific product of myeloperoxidase, potently inactivates cathepsin G by a pathway that involves oxidation of a specific methionine residue, which in turn may disrupt the catalytic charge relay system and introduce proteolytic cleavage sites into the enzyme. This finding raises the possibility that myeloperoxidase might restrain the activity of cathepsin G near the surface of neutrophils	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
sputum	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	hypochlorous acid, a specific product of myeloperoxidase, potently inactivates cathepsin G by a pathway that involves oxidation of a specific methionine residue, which in turn may disrupt the catalytic charge relay system and introduce proteolytic cleavage sites into the enzyme. This finding raises the possibility that myeloperoxidase might restrain the activity of cathepsin G near the surface of neutrophils	Homo sapiens	?	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)