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Literature summary for 1.3.5.1 extracted from

  • Mogi, T.; Kawakami, T.; Arai, H.; Igarashi, Y.; Matsushita, K.; Mori, M.; Shiomi, K.; Omura, S.; Harada, S.; Kita, K.
    Siccanin rediscovered as a species-selective succinate dehydrogenase inhibitor (2009), J. Biochem., 146, 383-387.
    View publication on PubMed

Application

Application Comment Organism
medicine species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics Mus musculus
medicine species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics Escherichia coli
medicine species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics Rattus norvegicus
medicine species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics Pseudomonas aeruginosa
medicine species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics Pseudomonas putida
medicine species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics Corynebacterium glutamicum

Inhibitors

Inhibitors Comment Organism Structure
additional information residual activity: 97%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site Corynebacterium glutamicum
additional information residual activity: above 77%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site Escherichia coli
siccanin
-
Escherichia coli
siccanin residual activity: 7%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site Mus musculus
siccanin residual activity: 13%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site Pseudomonas aeruginosa
siccanin residual activity: above 1%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site Pseudomonas putida
siccanin residual activity: 19%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound enzyme is used Escherichia coli 16020
-
membrane membrane-bound enzyme is used Pseudomonas putida 16020
-
membrane membrane-bound SDH is used Pseudomonas aeruginosa 16020
-
membrane membrane-bound SDH is used Corynebacterium glutamicum 16020
-
mitochondrion
-
Mus musculus 5739
-
mitochondrion
-
Rattus norvegicus 5739
-

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum
-
-
-
Escherichia coli
-
-
-
Mus musculus
-
-
-
Pseudomonas aeruginosa
-
-
-
Pseudomonas putida
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Mus musculus
-
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquinone-1 + L-malate
-
Mus musculus ?
-
?
ubiquinone-1 + L-malate
-
Escherichia coli ?
-
?
ubiquinone-1 + L-malate
-
Rattus norvegicus ?
-
?
ubiquinone-1 + L-malate
-
Pseudomonas aeruginosa ?
-
?
ubiquinone-1 + L-malate
-
Pseudomonas putida ?
-
?
ubiquinone-1 + L-malate
-
Corynebacterium glutamicum ?
-
?
ubiquinone-1 + succinate
-
Mus musculus ubiquinol + fumarate
-
?
ubiquinone-1 + succinate
-
Rattus norvegicus ubiquinol + fumarate
-
?
ubiquinone-1 + succinate
-
Escherichia coli ubiquinol-1 + fumarate
-
?
ubiquinone-1 + succinate
-
Pseudomonas aeruginosa ubiquinol-1 + fumarate
-
?
ubiquinone-1 + succinate
-
Pseudomonas putida ubiquinol-1 + fumarate
-
?
ubiquinone-1 + succinate
-
Corynebacterium glutamicum ubiquinol-1 + fumarate
-
?

Synonyms

Synonyms Comment Organism
SDH
-
Mus musculus
SDH
-
Escherichia coli
SDH
-
Rattus norvegicus
SDH
-
Pseudomonas aeruginosa
SDH
-
Pseudomonas putida
SDH
-
Corynebacterium glutamicum
succinate dehydrogenase
-
Mus musculus
succinate dehydrogenase
-
Escherichia coli
succinate dehydrogenase
-
Rattus norvegicus
succinate dehydrogenase
-
Pseudomonas aeruginosa
succinate dehydrogenase
-
Pseudomonas putida
succinate dehydrogenase
-
Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Mus musculus
25
-
assay at Escherichia coli
25
-
assay at Rattus norvegicus
25
-
assay at Pseudomonas aeruginosa
25
-
assay at Pseudomonas putida
25
-
assay at Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Mus musculus
7.4
-
assay at Escherichia coli
7.4
-
assay at Rattus norvegicus
7.4
-
assay at Pseudomonas aeruginosa
7.4
-
assay at Pseudomonas putida
7.4
-
assay at Corynebacterium glutamicum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0009
-
pH 7.4, 25°C Pseudomonas aeruginosa siccanin
0.009
-
pH 7.4, 25°C Rattus norvegicus siccanin
0.21
-
-
Escherichia coli siccanin