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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.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
(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

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

Synonyms

Synonyms Comment Organism
Sap2p
-
Candida albicans
Sapp1p
-
Candida parapsilosis
Sapt1p
-
Candida tropicalis
secreted aspartic protease
-
Candida albicans
secreted aspartic protease
-
Candida parapsilosis
secreted aspartic protease
-
Candida tropicalis