Literature summary for 3.4.23.24 extracted from

Majer, F.; Pavlickova, L.; Majer, P.; Hradilek, M.; Dolejsi, E.; Hruskova-Heidingsfeldova, O.; Pichova, I.
Structure-based specificity mapping of secreted aspartic proteases of Candida parapsilosis, Candida albicans, and Candida tropicalis using peptidomimetic inhibitors and homology modeling (2006), Biol. Chem., 387, 1247-1254.

Inhibitors

Inhibitors	Comment	Organism
(2R,3S)-phenylnorstatine	the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative	Candida albicans
(2R,3S)-phenylnorstatine	the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative	Candida parapsilosis
(2R,3S)-phenylnorstatine	the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative	Candida tropicalis
(2S,3S)-phenylnorstatine	the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative	Candida albicans
(2S,3S)-phenylnorstatine	the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative	Candida parapsilosis
(2S,3S)-phenylnorstatine	the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative	Candida tropicalis
(3S,4S)-phenylstatine	-	Candida albicans
(3S,4S)-phenylstatine	-	Candida parapsilosis
(3S,4S)-phenylstatine	-	Candida tropicalis
(3S,4S)-statine	-	Candida albicans
(3S,4S)-statine	-	Candida parapsilosis
(3S,4S)-statine	-	Candida tropicalis

Organism	UniProt	Comment	Textmining
Candida albicans	P0DJ06	-	-
Candida parapsilosis	P32951	-	-
Candida tropicalis	Q00663	-	-