Literature summary for 3.4.14.5 extracted from

Rigolet, P.; Mechin, I.; Delage, M.M.; Chich, J.F.
The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis (2002), Structure, 10, 1383-1394.

Search for more literature for 3.4.14.5

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Lactococcus lactis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, hanging drop method using 5-10% PEG 4000, pH 5.2, 18°C, preparation of heavy atom derivatives, X-ray diffraction structure determination and analysis at 2.2 A resolution	Lactococcus lactis

Organism

Organism	UniProt	Comment	Textmining
Lactococcus lactis	P22346	ssp. cremoris	-
Lactococcus lactis	Q9CE11	ssp. cremoris	-

Reaction

Reaction	Comment	Organism	Reaction ID
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline	active site structure and accessibility	Lactococcus lactis	a

Subunits

Subunits	Comment	Organism
dimer	homodimeric enzyme, crystal structure, overall fold and structure of the dimer and dimer interface, overview	Lactococcus lactis

Synonyms

Synonyms	Comment	Organism
More	enzyme belongs to the SC clan that includes 38 families of peptidases, and is the prototype of the S15 family	Lactococcus lactis
PepX	-	Lactococcus lactis
X-PDAP	-	Lactococcus lactis
X-prolyl dipeptidyl aminopeptidase	-	Lactococcus lactis

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Release 2023.1 (January 2023)