Functional and comparative analysis of the FeII/2-oxoglutarate-dependent dioxygenases without using any substrate
Non-haem iron (FeII) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation of 2OG to the hydroxylation of the substrates. While some of these enzymes are reported to have multiple substrates, the substrate remains unk...
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| Published in | Biology methods and protocols Vol. 10; no. 1; p. bpae096 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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01.01.2025
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| ISSN | 2396-8923 2396-8923 |
| DOI | 10.1093/biomethods/bpae096 |
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| Abstract | Non-haem iron (FeII) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation of 2OG to the hydroxylation of the substrates. While some of these enzymes are reported to have multiple substrates, the substrate remains unknown for many of the enzymes. However, in the absence of the substrate, these enzymes catalyse oxidative decarboxylation of 2OG and generate succinate. We have determined succinate level to monitor this uncoupled reaction and compared the uncoupled 2OG turnover of different FeII/2OG-dependent dioxygenases. The uncoupled succinate production was used to verify the NiII-mediated inhibition and functionality of human dioxygenase ALKBH6. |
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| AbstractList | Non-haem iron (FeII) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation of 2OG to the hydroxylation of the substrates. While some of these enzymes are reported to have multiple substrates, the substrate remains unknown for many of the enzymes. However, in the absence of the substrate, these enzymes catalyse oxidative decarboxylation of 2OG and generate succinate. We have determined succinate level to monitor this uncoupled reaction and compared the uncoupled 2OG turnover of different FeII/2OG-dependent dioxygenases. The uncoupled succinate production was used to verify the NiII-mediated inhibition and functionality of human dioxygenase ALKBH6. Non-haem iron (Fe II ) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation of 2OG to the hydroxylation of the substrates. While some of these enzymes are reported to have multiple substrates, the substrate remains unknown for many of the enzymes. However, in the absence of the substrate, these enzymes catalyse oxidative decarboxylation of 2OG and generate succinate. We have determined succinate level to monitor this uncoupled reaction and compared the uncoupled 2OG turnover of different Fe II /2OG-dependent dioxygenases. The uncoupled succinate production was used to verify the Ni II -mediated inhibition and functionality of human dioxygenase ALKBH6. Non-haem iron (FeII) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation of 2OG to the hydroxylation of the substrates. While some of these enzymes are reported to have multiple substrates, the substrate remains unknown for many of the enzymes. However, in the absence of the substrate, these enzymes catalyse oxidative decarboxylation of 2OG and generate succinate. We have determined succinate level to monitor this uncoupled reaction and compared the uncoupled 2OG turnover of different FeII/2OG-dependent dioxygenases. The uncoupled succinate production was used to verify the NiII-mediated inhibition and functionality of human dioxygenase ALKBH6.Non-haem iron (FeII) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation of 2OG to the hydroxylation of the substrates. While some of these enzymes are reported to have multiple substrates, the substrate remains unknown for many of the enzymes. However, in the absence of the substrate, these enzymes catalyse oxidative decarboxylation of 2OG and generate succinate. We have determined succinate level to monitor this uncoupled reaction and compared the uncoupled 2OG turnover of different FeII/2OG-dependent dioxygenases. The uncoupled succinate production was used to verify the NiII-mediated inhibition and functionality of human dioxygenase ALKBH6. |
| Author | Das, Susmita Shahnaz, Nafeesa Keerthana, Carmel Tuti, Nikhil Meur, Gargi Shaji, Unnikrishnan P Ranjan, Saumya Seenivasan, Gayathri Anindya, Roy |
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| Snippet | Non-haem iron (FeII) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation... Non-haem iron (Fe II ) and 2-oxoglutarate(2OG)-dependent dioxygenases catalyse various biological reactions. These enzymes couple the oxidative decarboxylation... |
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| SubjectTerms | Chromatography Cloning Comparative analysis Decarboxylation Dioxygenase DNA repair E coli Enzymes Genes Hydroxylation Ketoglutaric acid Mass spectrometry Methods Mutagenesis Polypeptides Proteins Scientific imaging |
| Title | Functional and comparative analysis of the FeII/2-oxoglutarate-dependent dioxygenases without using any substrate |
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