Literature summary for 3.2.1.166 extracted from

Hulett, M.D.; Hornby, J.R.; Ohms, S.J.; Zuegg, J.; Freeman, C.; Gready, J.E.; Parish, C.R.
Identification of active-site residues of the pro-metastatic endoglycosidase heparanase (2000), Biochemistry, 39, 15659-15667.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in COS-7 cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D367A	mutant enzyme is not expressed	Homo sapiens
Q225A	mutation results in the complete loss of heparanase activity	Homo sapiens
Q343A	mutation results in the complete loss of heparanase activity	Homo sapiens
Q378A	mutation does not reduce activity	Homo sapiens
Q396A	mutation does not reduce activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y251	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
heparan sulfate + H2O	catalytic mechanism that involves two conserved acidic residues, a putative proton donor at Glu225 and a nucleophile at Glu343	Homo sapiens	heparan sulfate fragment + truncated heparan sulfate proteoglycan	-	?

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Release 2023.1 (January 2023)