Literature summary for 3.4.21.66 extracted from

Stepanov, V.M.; Chestukhina, G.G.; Rudenskaya, G.N.; Epremyan, A.S.; Osterman, A.L.; Khodova, O.M.; Belyanova, L.P.
A new subfamily of microbial serine proteinase? Structural similarities of Bacillus thuringiensis and Thermoactinomyces vulgaris extracellular serine proteinases (1981), Biochem. Biophys. Res. Commun., 100, 1680-1687.

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Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	cysteine residues essential for activity	Thermoactinomyces vulgaris

Inhibitors

Inhibitors	Comment	Organism	Structure
p-chloromercuribenzoate	-	Thermoactinomyces vulgaris
PMSF	-	Thermoactinomyces vulgaris

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Thermoactinomyces vulgaris	-	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
28000	-	Thermoactinomyces vulgaris	Thermoactinomyces vulgaris

Organism

Organism	UniProt	Comment	Textmining
Thermoactinomyces vulgaris	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Benzyloxycarbonyl-L-Ala-L-Ala-L-Leu 4-nitroanilide + H2O	-	Thermoactinomyces vulgaris	?	-	?

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
additional information	-	pI: 8-9	Thermoactinomyces vulgaris
8.2	-	benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide	Thermoactinomyces vulgaris

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Release 2023.1 (January 2023)