Literature summary for 3.4.21.B48 extracted from

Oyama, H.; Hamada, T.; Ogasawara, S.; Uchida, K.; Murao, S.; Beyer, B.B.; Dunn, B.M.; Oda, K.
A CLN2-related and thermostable serine-carboxyl proteinase, kumamolysin: cloning, expression, and identification of catalytic serine residue (2002), J. Biochem., 131, 757-765.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus novosp.

Protein Variants

Protein Variants	Comment	Organism
additional information	mutational analysis of the Ser278 residue reveals that the mutant loses both auto-processing activity and proteolytic activity	Bacillus novosp.

Inhibitors

Inhibitors	Comment	Organism	Structure
acetyl-Ile-Pro-Phe-CHO	-	Bacillus novosp.

Organism

Organism	UniProt	Comment	Textmining
Bacillus novosp.	-	MN-32	-
Bacillus novosp. MN-32	-	MN-32	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the enzyme is synthesiszed as a larger precursor consisting of two regions: amino-terminal prepro (199 amino acids) and mature proteins (384 amino acids)	Bacillus novosp.

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	-	Bacillus novosp.

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Release 2023.1 (January 2023)