Literature summary for 3.4.21.12 extracted from

Derman, A.I.; Agard, D.A.
Two energetically disparate folding pathways of alpha-lytic protease share a single transition state (2000), Nat. Struct. Biol., 7, 394-397.

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Cloned(Commentary)

Cloned (Comment)	Organism
mutant enzyme precursor with a pro region lacking its last three amino acids: the turnover number of folding of the mutant enzyme is 1000fold lower that for the folding of the wild type enzyme. Mutant enzyme precursor with a pro region lacking its last three amino acids and two additional mutations, R102H and G134S: turnover number of folding of the mutant enzyme is 2fold higher than that of the wild-type enzyme	Lysobacter enzymogenes

Cloned (Comment)

Organism

mutant enzyme precursor with a pro region lacking its last three amino acids: the turnover number of folding of the mutant enzyme is 1000fold lower that for the folding of the wild type enzyme. Mutant enzyme precursor with a pro region lacking its last three amino acids and two additional mutations, R102H and G134S: turnover number of folding of the mutant enzyme is 2fold higher than that of the wild-type enzyme

Lysobacter enzymogenes

Organism

Organism	UniProt	Comment	Textmining
Lysobacter enzymogenes	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the enzyme is synthesized with a 166 amino acid pro region that catalyzes the folding of the 198 amino acid protease into its native conformation.	Lysobacter enzymogenes

Synonyms

Synonyms	Comment	Organism
alpha-lytic protease	-	Lysobacter enzymogenes
alphaLP	-	Lysobacter enzymogenes

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Release 2023.1 (January 2023)