Literature summary for 3.4.11.5 extracted from

Akioka, M.; Nakano, H.; Horikiri, A.; Tsujimoto, Y.; Matsui, H.; Shimizu, T.; Nakatsu, T.; Kato, H.; Watanabe, K.
Overexpression, purification, crystallization and preliminary X-ray crystallographic studies of a proline-specific aminopeptidase from Aneurinibacillus sp. strain AM-1 (2006), Acta Crystallogr. Sect. F, 62, 1266-1268.

Search for more literature for 3.4.11.5

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Aneurinibacillus sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
native enzyme and selenomethionine derivative in the resolution range between 20-2.1 A. Space group P212121	Aneurinibacillus sp.

Organism

Organism	UniProt	Comment	Textmining
Aneurinibacillus sp.	A2V759	-	-
Aneurinibacillus sp. am-1	A2V759	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	N-terminal region from amino-acid positions 1-27 functions as a signal sequence for secretion	Aneurinibacillus sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
5.5	-	-	Aneurinibacillus sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-prolyl-4-nitroanilide + H2O	-	Aneurinibacillus sp.	L-proline + 4-nitroaniline	-	?
L-prolyl-4-nitroanilide + H2O	-	Aneurinibacillus sp. am-1	L-proline + 4-nitroaniline	-	?

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Release 2023.1 (January 2023)