Functional characterization of X-prolyl aminopeptidase from Toxoplasma gondii.

Abstract:

:In the present study, a recombinant aminopeptidase P (rTgAPP) from Toxoplasma gondii was expressed in Escherichia coli to evaluate its enzyme parameters. The rTgAPP showed strong activity against a synthetic substrate for aminopeptidase P at pH 8·0 with a K m value of 0·255 µ m and a k cat value of 35·6 s-1. The overall catalytic efficiency (k cat/K m) of the rTgAPP was 139·6 × 105 M-1 s-1. The activity of rTgAPP was enhanced by the addition of divalent cations and inhibited by bestatin. Deletion of TgAPP gene in the parasite through a CRISPR/Cas9 system resulted in inhibition of growth indicating the importance of TgAPP. Thus our findings reveal that TgAPP is an active enzyme in T. gondii and provide an insight into the function of TgAPP.

journal_name

Parasitology

journal_title

Parasitology

authors

Yang M,Zheng J,Jia H,Song M

doi

10.1017/S0031182016000986

subject

Has Abstract

pub_date

2016-09-01 00:00:00

pages

1443-9

issue

11

eissn

0031-1820

issn

1469-8161

pii

S0031182016000986

journal_volume

143

pub_type

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