Literature summary for 3.4.21.34 extracted from

Tang, J.; Yu, C.L.; Williams, S.R.; Springman, E.; Jeffery, D.; Sprengeler, P.A.; Estevez, A.; Sampang, J.; Shrader, W.; Spencer, J.; Young, W.; McGrath, M.; Katz, B.A.
Expression, crystallization, and three-dimensional structure of the catalytic domain of human plasma kallikrein (2005), J. Biol. Chem., 280, 41077-41089.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of the protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase to reduce heterogeneity from the glycosylation. In the baculovirus/Sf9 system, homogenous, crystallizable, and nonglycosylated protein is expressed after mutagenizing three asparagines to glutamate. The activity of the catalytic domain is similar to that of the full-length protein	Homo sapiens

Cloned (Comment)

Organism

expression of the protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase to reduce heterogeneity from the glycosylation. In the baculovirus/Sf9 system, homogenous, crystallizable, and nonglycosylated protein is expressed after mutagenizing three asparagines to glutamate. The activity of the catalytic domain is similar to that of the full-length protein

Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
protease domain recombinantly expressed in Pichia pastoris or in the baculovirus/Sf9 system. Structure for the endoglycosidase H-deglycosylated protease domain produced from Pichia pastoris is determined at 1.4 A. Structure for the mutagenically deglycosylated form produced from Sf9 cells is determined at 1.4 A	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.091	-	D-butyl-cyclohexylalanine-arginine-4-nitroanilide	catalytic domain expressed after mutagenizing three asparagines to glutamate in a baculovirus/Sf9 system	Homo sapiens
0.108	-	D-butyl-cyclohexylalanine-arginine-4-nitroanilide	full-length kallikrein	Homo sapiens
0.117	-	D-butyl-cyclohexylalanine-arginine-4-nitroanilide	protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q92876	-	-

Purification (Commentary)

Purification (Comment)	Organism
protease domain recombinantly expresed in Pichia pastoris or in the baculovirus/Sf9 system	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-butyl-cyclohexylalanine-arginine-4-nitroanilide + H2O	-	Homo sapiens	D-butyl-cyclohexylalanine-arginine + 4-nitroaniline	-	?
N-butyl-(R)-cyclohexylalanyl-L-Arg-p-nitroanilide + H2O	i.e. Pefachrome PK	Homo sapiens	N-butyl-(R)-cyclohexylalanyl-L-Arg + p-nitroaniline	-	?