Literature summary for 3.4.22.10 extracted from

Lane, M.D.; Seelig, B.
Highly efficient recombinant production and purification of streptococcal cysteine protease streptopain with increased enzymatic activity (2016), Protein Expr. Purif., 121, 66-72 .

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Cloned(Commentary)

Cloned (Comment)	Organism
production of large quantities of soluble streptopain using the autoinduction method for Escherichia coli recombinant protein expression with a C-terminal His6 tag. Soluble streptopain is obtained as mature enzyme, indicating that at some point during autoinduction or cell lysis, the protease must have become active. If incubated long enough after lysis, the protease digestes most proteins in the lysate	Streptococcus pyogenes

Cloned (Comment)

Organism

production of large quantities of soluble streptopain using the autoinduction method for Escherichia coli recombinant protein expression with a C-terminal His6 tag. Soluble streptopain is obtained as mature enzyme, indicating that at some point during autoinduction or cell lysis, the protease must have become active. If incubated long enough after lysis, the protease digestes most proteins in the lysate

Streptococcus pyogenes

Organism

Organism	UniProt	Comment	Textmining
Streptococcus pyogenes	P0C0J0	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	streptopain is initially expressed as a 40 kDa zymogen. Maturation is caused by cleavage of the 138 N-terminal amino acids, resulting in a 28000 active protease	Streptococcus pyogenes

Purification (Commentary)

Purification (Comment)	Organism
a combination of two successive strong cation exchange resins gives the best results for soluble, pure enzyme with the highest activity	Streptococcus pyogenes

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
FAAIKAGARY + H2O	-	Streptococcus pyogenes	FAAIK + AGARY	-	?
additional information	streptopain can cleave a wide range of human proteins, including immunoglobulins, the complement activation system, chemokines, and structural proteins	Streptococcus pyogenes	?	-	?

Synonyms

Synonyms	Comment	Organism
SpeB	-	Streptococcus pyogenes

General Information

General Information	Comment	Organism
physiological function	streptopain is a critical virulence factor for pathogenesis	Streptococcus pyogenes