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Literature summary for 2.3.1.B43 extracted from

  • Ren, Z.; Dong, X.; Guan, L.; Yang, L.; Liu, C.; Cai, X.; Hu, H.; Lv, Z.; Liu, H.; Zheng, L.; Huang, J.; Wilson, R.A.; Chen, X.L.
    Sirt5-mediated lysine desuccinylation regulates oxidative stress adaptation in Magnaporthe oryzae during host intracellular infection (2024), New Phytol., 242, 1257-1274.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Pyricularia oryzae 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[glutathione peroxidase Hyr1]-N6-succinyl-L-lysine + NAD+ + H2O Pyricularia oryzae Sirt5 desuccinylates glutathione peroxidase Hyr1 to activate its enzyme activity, likely by affecting proper folding [glutathione peroxidase Hyr1]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[thioredoxin Trx2]-N6-succinyl-L-lysine + NAD+ + H2O Pyricularia oryzae Sirt5 desuccinylates thioredoxin Trx2 to activate its enzyme activity, likely by affecting proper folding [thioredoxin Trx2]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?

Organism

Organism UniProt Comment Textmining
Pyricularia oryzae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
conidium
-
Pyricularia oryzae
-
hypha
-
Pyricularia oryzae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[COA6]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [COA6]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[COX12]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [COX12]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[COX5A]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [COX5A]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[COX5B]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [COX5B]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[glutathione peroxidase Hyr1]-N6-succinyl-L-lysine + NAD+ + H2O Sirt5 desuccinylates glutathione peroxidase Hyr1 to activate its enzyme activity, likely by affecting proper folding Pyricularia oryzae [glutathione peroxidase Hyr1]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[glutathione peroxidase Hyr1]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [glutathione peroxidase Hyr1]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[Ndufa2]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [Ndufa2]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[Ndufa8]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [Ndufa8]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[Ndufs4]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [Ndufs4]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[Ndufs6]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [Ndufs6]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[thioredoxin Trx2]-N6-succinyl-L-lysine + NAD+ + H2O Sirt5 desuccinylates thioredoxin Trx2 to activate its enzyme activity, likely by affecting proper folding Pyricularia oryzae [thioredoxin Trx2]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?
[thioredoxin Trx2]-N6-succinyl-L-lysine + NAD+ + H2O
-
Pyricularia oryzae [thioredoxin Trx2]-L-lysine + 2''-O-succinyl-ADP-D-ribose + nicotinamide
-
?

Synonyms

Synonyms Comment Organism
SIRT5
-
Pyricularia oryzae

General Information

General Information Comment Organism
malfunction deletion of SIRT5 results in hypersuccinylation of detoxification-related enzymes, and significant reduction in NADPH:NADP+ and GSH:GSSG ratios, disrupting redox balance and impeding invasive growth Pyricularia oryzae
physiological function the desuccinylase is important for virulence via adaptation to host oxidative stress. Importance of Sirt5-mediated desuccinylation in controlling fungal process required for detoxifying host ROS during Pyricularia oryzae infection. Sirt5 desuccinylates thioredoxin Trx2 and glutathione peroxidase Hyr1 to activate their enzyme activity, likely by affecting proper folding Pyricularia oryzae