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. Author manuscript; available in PMC: 2014 Mar 14.
Published in final edited form as: Adv Exp Med Biol. 2011;712:49–61. doi: 10.1007/978-1-4419-8414-2_4

Table I.

Features of T. gondii cathepsin-like proteases.

Protease Length
(aa)		 Catalytic
domain1 		Mature
MW		 Activity3 Chromo-
some		 Exons Optimal
pH		 Activation Stage Expression Substrate
specificity
TgCPL 422 206–420 30 kDa Endo Ib 4 5.5–6.0 (polypeptide) 6.5 (synthetic peptides) Autoactivation in vitro Tachyzoite and bradyzoite P2 hydrophobic
TgCPB 569 275–532 28 kDa Endo/Exo XII 7 ND Autoactivation in vitro Tachyzoite and bradyzoite (microarray analysis) P2 hydrophobic
TgCPC1 733 412–709 35 kDa2 Exo IX 9 6.5 No autoactivation in vitro Tachyzoite 17-fold higher activity for Gly-Arg than human cathepsin-C specific substrate Gly-Phe
TgCPC2 753 357–630 44 kDa2 Exo III 10 ND No autoactivation in vitro Tachyzoite ND
TgCPC3 622 335–647 32 kDa2 Exo IX 14 ND ND Sporozoite (expressed sequence tags) ND
1

Numbered from the initiator methionine.

2

MW is based on the size of the catalytic domain without further processing into the heavy and light chains, if occurring.

3

Endo, endopeptidase; Exo, exopeptidase