Literature summary for 3.2.1.35 extracted from

Deschrevel, B.; Tranchepain, F.; Vincent, J.C.
Chain-length dependence of the kinetics of the hyaluronan hydrolysis catalyzed by bovine testicular hyaluronidase (2008), Matrix Biol., 27, 475-486.

Search for more literature for 3.2.1.35

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Km strongly decreases with increasing HA chain sizes	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
testis	-	Bos taurus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
hyaluronan + H2O	hyaluronan fragments are used with a molar mass ranging from 800 g/mol to 250000 g/mol and native hyaluronan to study the influence of the chain length of hyaluronan on the kinetics of its HAase-catalyzed hydrolysis. The initial hydrolysis rate strongly varies with hyaluronan chain length. The ability of HA chains to form an efficient enzyme-substrate complex is maximum for hyaluronan molar masses ranging from 3000 to 20000 g/mol. Shorter hyaluronan chains are too short to form a stable complex and longer hyaluronan chains encounter difficulties in forming a complex, due to steric hindrance. As the chain length decreases the HAase increasingly catalyses transglycosylation rather than hydrolysis. Two hyaluronan chain populations, corresponding to hyaluronan chain molar masses lower and higher than approximately 20000 g/mol are identified and related to the bi-exponential character	Bos taurus	?	-	?

Synonyms

Synonyms	Comment	Organism
hyaluronidase	-	Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Bos taurus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5	-	assay at	Bos taurus

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Release 2023.1 (January 2023)