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Information on EC 3.4.23.24 - Candidapepsin and Organism(s) Candida tropicalis and UniProt Accession Q00663

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.24 Candidapepsin
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This record set is specific for:
Candida tropicalis
UNIPROT: Q00663 not found.
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Word Map
The taxonomic range for the selected organisms is: Candida tropicalis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of insulin B chain. Activates trypsinogen, and degrades keratin
Synonyms
aspartyl protease, secreted aspartyl proteinase, sap11, secreted aspartyl proteinases, sapp1p, sap10, yapsin, secreted aspartic proteinase, secreted aspartic protease, sap1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
secreted aspartic protease
-
Aspartate protease
-
-
-
-
Candida albicans aspartic proteinase
-
-
-
-
Candida albicans carboxyl proteinase
-
-
-
-
Candida albicans secretory acid proteinase
-
-
-
-
Candida olea acid proteinase
-
-
-
-
Proteinase, Candida albicans aspartic
-
-
-
-
Proteinase, Candida aspartic
-
-
-
-
Proteinase, Candida olea aspartic
-
-
-
-
S-aspartyl proteinase
-
-
SAP2
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isoform
SAP4
-
isoform
SAPT1
-
isozyme
SAPT2
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isozyme
SAPT3
-
isozyme
SAPT4
-
isozyme
secreted aspartyl protease
-
-
secreted aspartyl proteinase
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
69458-91-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R,3S)-phenylnorstatine
the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative
(2S,3S)-phenylnorstatine
the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative
(3S,4S)-phenylstatine
-
(3S,4S)-statine
-
mycogenic silver nanoparticles
-
after 24 h of incubation, significant reduction (56%) in metabolic activity is observed with 100ppm mycogenic silver nanoparticles
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pepstatin A
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
secreted aspartyl proteinases are not involved in invasion and damage of reconstituted human oral epithelium by Candida tropicalis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CARP_CANTR
394
0
42559
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Top-10 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
combination of fluconazole with clotrimazole can cause a down-regulation of gene expression of isoforms SAP2 and SAP4
-
SAPT2-4 transcripts are frequently detected 12 h after infection of reconstituted human oral epithelium
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Biol. Chem.
387
1247-1254
2006
Candida albicans (P0DJ06), Candida albicans, Candida parapsilosis (P32951), Candida parapsilosis, Candida tropicalis (Q00663), Candida tropicalis
Manually annotated by BRENDA team
Parra-Ortega, B.; Cruz-Torres, H.; Villa-Tanaca, L.; Hernandez-Rodriguez, C.
Phylogeny and evolution of the aspartyl protease family from clinically relevant Candida species
Mem. Inst. Oswaldo Cruz
104
505-512
2009
Candida albicans, Pichia kudriavzevii, [Candida] glabrata, Meyerozyma guilliermondii, Kluyveromyces marxianus, Candida parapsilosis, Candida tropicalis, Clavispora lusitaniae, Candida dubliniensis
Manually annotated by BRENDA team
Silva, S.; Hooper, S.J.; Henriques, M.; Oliveira, R.; Azeredo, J.; Williams, D.W.
The role of secreted aspartyl proteinases in Candida tropicalis invasion and damage of oral mucosa
Clin. Microbiol. Infect.
17
264-272
2011
Candida tropicalis
Manually annotated by BRENDA team
Hamid, S.; Zainab, S.; Faryal, R.; Ali, N.; Sharafat, I.
Inhibition of secreted aspartyl proteinase activity in biofilms of Candida species by mycogenic silver nanoparticles
Artif. Cells Nanomed. Biotechnol.
46
551-557
2018
Candida albicans, Pichia kudriavzevii, [Candida] glabrata, Candida parapsilosis, Candida tropicalis
Manually annotated by BRENDA team
Khodavandi, A.; Alizadeh, F.; Abdolahi, M.; Jahangiri, M.
Differential expression levels of agglutinin-like sequence, lipase, and secreted aspartyl protease genes in Candida tropicalis treated with fluconazole alone and in combination with clotrimazole
J. Rep. Pharma. Sci.
8
28-33
2019
Candida tropicalis, Candida tropicalis ATCC 750
-
Manually annotated by BRENDA team