Literature summary for 3.4.21.19 extracted from

Meijers, R.; Blagova, E.V.; Levdikov, V.M.; Rudenskaya, G.N.; Chestukhina, G.G.; Akimkina, T.V.; Kostrov, S.V.; Lamzin, V.S.; Kuranova, I.P.
The crystal structure of glutamyl endopeptidase from Bacillus intermedius reveals a structural link between zymogen activation and charge compensation (2004), Biochemistry, 43, 2784-2791.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme in 0.01 M Tris-HCl, pH 7.0, 2 mM CaCl2, 1.2 M potassium phosphate, with or without 3% 2-methyl-2,4-pentanediol, presence of the latter leads to a second crystal form, X-ray diffraction structure determination and analysis at 1.5-1.75 A resolution	Bacillus intermedius

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Bacillus intermedius	-	-

Organism

Organism	UniProt	Comment	Textmining
Bacillus intermedius	-	chymotrypsin-like serine protease	-

Reaction

Reaction	Comment	Organism	Reaction ID
Preferential cleavage: Glu-/-, Asp-/-	specific for cleavage on the carboxylic site of glutamic acid, catalytic site are His47 and Ser171, the N-terminus is involved in formation of the substrate binding pocket, a direct structural relation between zymogen activation and substrate charge compensation exists	Bacillus intermedius	a

Synonyms

Synonyms	Comment	Organism
BIEP	-	Bacillus intermedius
Glu-endopeptidase	-	Bacillus intermedius
glutamyl specific endopeptidase	-	Bacillus intermedius

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Release 2023.1 (January 2023)