Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fedotcheva, N.; Kondrashova, M.; Litvinova, E.; Zakharchenko, M.; Khunderyakova, N.; Beloborodova, N.
    Modulation of the activity of succinate dehydrogenase by acetylation with chemicals, drugs, and microbial metabolites (2018), Biophysics, 63, 743-750 .
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.5.1 Acetylsalicylic acid
-
 Rattus norvegicus
1.3.5.1 malonate a specific inhibitor of SDH Rattus norvegicus
1.3.5.1 additional information inhibitory effects of acetylating and deacetylating compounds on the activity of succinate dehydrogenase, as well as effects on the membrane potential and calcium retention capacity of the isolated liver mitochondria, and determination of the possible sites of the enzyme inhibition by the acetylating compounds, overview. Acetylsalicylic acid is the most effective inhibitor of SDH. The inhibition of the enzyme is due to the acetylation of the site binding alpha-ketoglutarate, and it is partially eliminated or prevented by pre-incubation of the mitochondria with nicotinamide adenine dinucleotide, a cofactor for deacetylation, and with polyamine spermidine, an acceptor of acetyl groups. Malonate and thenoyltrifluoroacetate (TTFA), which are specific inhibitors of SDH, as well as the intermediate carrier of electrons phenazine methosulfate (PMS), are used to identify the possible sites of action of these compounds. The influence of NAD, as a cofactor in deacetylation, and polyamine spermidine, as a possible activator of deacetylation, on the modulation of the activity of SDH by acetylating compounds is investigated. PMS prevents the inhibition of SDH caused by TTFA and has no effect on the inhibition induced by malonate. PMS almost completely prevents the inhibition induced by the tested compounds, as does NAD Rattus norvegicus
1.3.5.1 N-acetylcysteine
-
 Rattus norvegicus
1.3.5.1 N-Acetylimidazole
-
 Rattus norvegicus
1.3.5.1 phenylacetate unlike N-acetylimidazole and acetylsalicylic acid, phenylacetate is not a donor of acetyl groups. It can be assumed that its effect on SDH may be due to both the activation of acetylation and direct interaction with the enzyme Rattus norvegicus
1.3.5.1 thenoyltrifluoroacetate TTFA, a specific inhibitor of SDH Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.1 mitochondrion
-
 Rattus norvegicus 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.1 succinate + a quinone Rattus norvegicus
-
 fumarate + a quinol
-
 ?
1.3.5.1 succinate + a quinone Rattus norvegicus Wistar
-
 fumarate + a quinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Rattus norvegicus Q920L2
-
-
1.3.5.1 Rattus norvegicus Wistar Q920L2
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.5.1 liver from male rats Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 additional information determination of the activity of succinate dehydrogenase by 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenyl-tetrazolium bromide reduction and by reduction of electron acceptor dichlorophenolindophenol (DCPIP) Rattus norvegicus ?
-
-
1.3.5.1 additional information determination of the activity of succinate dehydrogenase by 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenyl-tetrazolium bromide reduction and by reduction of electron acceptor dichlorophenolindophenol (DCPIP) Rattus norvegicus Wistar ?
-
-
1.3.5.1 succinate + a quinone
-
 Rattus norvegicus fumarate + a quinol
-
 ?
1.3.5.1 succinate + a quinone
-
 Rattus norvegicus Wistar fumarate + a quinol
-
 ?
1.3.5.1 succinate + ubiquinone
-
 Rattus norvegicus fumarate + ubiquinol
-
 ?
1.3.5.1 succinate + ubiquinone
-
 Rattus norvegicus Wistar fumarate + ubiquinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.5.1 succinate dehydrogenase
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.5.1 22
-
 assay at room temperature Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.5.1 7.4
-
 assay at Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 FAD
-
 Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.3.5.1 physiological function acetylation can participate in the modulation of the enzymatic activity of SDH, a key enzyme of the tricarboxylic acid cycle, along with the well-known mechanisms of inhibition by oxaloacetic acid, oxidative stress, or mutations in enzyme subunits, in maintaining the energy supply, membrane potential, and other functions of mitochondria Rattus norvegicus