Literature summary for 3.4.21.109 extracted from

Miyake, Y.; Tsuzuki, S.; Mochida, S.; Fushiki, T.; Inouye, K.
The role of asparagine-linked glycosylation site on the catalytic domain of matriptase in its zymogen activation (2010), Biochim. Biophys. Acta, 1804, 156-165.

Search for more literature for 3.4.21.109

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in mammalian cells as a full-length rat matriptase with Myc-epitope-hexahistidine tag at its carboxyl-terminus	Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
additional information	a construct consisting of the catalytic domain of matriptase fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus shows comparable kinetic activity to the full-length rat matriptase toward peptide substrate methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide acetate	Rattus norvegicus
N772Q	Asn772 is N-glycosylated. Mutant N772Q consisting of the catalytic domain of matriptase bearing a N772Q mutation fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus is not detected in the medium conditioned by transfected cells but is on the cell surface and purified mutant N772Q exhibits markedly reduced activity toward peptide substrate methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide acetate	Rattus norvegicus
S805A	mutant is unable to undergo activation when expressed in MDCK cells	Rattus norvegicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.164	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase bearing a N772Q mutation fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase	Rattus norvegicus
0.188	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase	Rattus norvegicus
0.2	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	full-length rat matriptase with Myc-epitope-hexahistidine tag at its carboxyl-terminus	Rattus norvegicus
0.228	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase and glycopeptidase F	Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
33000	-	SDS-PAGE, reducing condition, protease inhibitor cocktail, Western blotting using an anti-myc antibody in a sample of medium, two bands 93 kDa and 33 kDa are visible, 33 kDa fragment is a cleavage product of the carboxyl-terminal part	Rattus norvegicus
43000	-	under non-reducing conditions in a sample of medium three bands 61 kDa, 55 kDa, 43 kDa are visible using Western blotting with a anti-myc antibody	Rattus norvegicus
55000	-	under non-reducing conditions in a sample of medium three bands 61 kDa, 55 kDa, 43 kDa are visible using Western blotting with a anti-myc antibody	Rattus norvegicus
61000	-	under non-reducing conditions in a sample of medium three bands 61 kDa, 55 kDa, 43 kDa are visible using Western blotting with a anti-myc antibody	Rattus norvegicus
93000	-	SDS-PAGE, reducing condition, protease inhibitor cocktail, Western blotting using an anti-myc antibody in a sample of medium, two bands 93 kDa and 33 kDa are visible. 93 kDa fragment represents released single-chain carboxyl-terminal part	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	catalytic domain is N-glycosylated at Asn772	Rattus norvegicus
proteolytic modification	matriptase is post-translationally processed by cleavage with unknown proteases between Gly149 and Ser150 within the sea-urchin sperm protein-enterokinase-agrin (SEA) domain	Rattus norvegicus

Purification (Commentary)

Purification (Comment)	Organism
purified from the conditioned medium using Ni-NTA chromatography	Rattus norvegicus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide + H2O	-	Rattus norvegicus	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine + p-nitroaniline	-	?

Synonyms

Synonyms	Comment	Organism
matriptase	-	Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.5	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase bearing a N772Q mutation fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase	Rattus norvegicus
59	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	full-length rat matriptase with Myc-epitope-hexahistidine tag at its carboxyl-terminus	Rattus norvegicus
91	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase	Rattus norvegicus
103	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase and glycopeptidase F	Rattus norvegicus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Rattus norvegicus

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
9.45	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase bearing a N772Q mutation fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase	Rattus norvegicus
290	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	full-length rat matriptase with Myc-epitope-hexahistidine tag at its carboxyl-terminus	Rattus norvegicus
454	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase and glycopeptidase F	Rattus norvegicus
484	-	methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide	construct consisting of the catalytic domain of matriptase fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase	Rattus norvegicus

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Release 2023.1 (January 2023)