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Article: Towards initial indications for a thiol-based redox control of arabidopsis 5-aminolevulinic acid dehydratase
Title | Towards initial indications for a thiol-based redox control of arabidopsis 5-aminolevulinic acid dehydratase |
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Authors | |
Keywords | ALAD Chlorophyll Posttranslational modification Redox control Tetrapyrrole biosynthesis Thioredoxins |
Issue Date | 2018 |
Citation | Antioxidants, 2018, v. 7, n. 11, article no. 152 How to Cite? |
Abstract | Thiol-based redox control is one of the important posttranslational mechanisms of the tetrapyrrole biosynthesis pathway. Many enzymes of the pathway have been shown to interact with thioredoxin (TRX) and Nicotinamide adenine dinucleotide phosphate (NADPH)-dependent thioredoxin reductase C (NTRC). We examined the redox-dependency of 5-aminolevulinic acid dehydratase (ALAD), which catalyzed the conjugation of two 5-aminolevulinic acid (ALA) molecules to porphobilinogen. ALAD interacted with TRX f, TRX m and NTRC in chloroplasts. Consequently, less ALAD protein accumulated in the trx f1, ntrc and trx f1/ntrc mutants compared to wild-type control resulting in decreased ALAD activity. In a polyacrylamide gel under non-reducing conditions, ALAD monomers turned out to be present in reduced and two oxidized forms. The reduced and oxidized forms of ALAD differed in their catalytic activity. The addition of TRX stimulated ALAD activity. From our results it was concluded that (i) deficiency of the reducing power mainly affected the in planta stability of ALAD; and (ii) the reduced form of ALAD displayed increased enzymatic activity. |
Persistent Identifier | http://hdl.handle.net/10722/316503 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Wittmann, Daniel | - |
dc.contributor.author | Kløve, Sigri | - |
dc.contributor.author | Wang, Peng | - |
dc.contributor.author | Grimm, Bernhard | - |
dc.date.accessioned | 2022-09-14T11:40:37Z | - |
dc.date.available | 2022-09-14T11:40:37Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Antioxidants, 2018, v. 7, n. 11, article no. 152 | - |
dc.identifier.uri | http://hdl.handle.net/10722/316503 | - |
dc.description.abstract | Thiol-based redox control is one of the important posttranslational mechanisms of the tetrapyrrole biosynthesis pathway. Many enzymes of the pathway have been shown to interact with thioredoxin (TRX) and Nicotinamide adenine dinucleotide phosphate (NADPH)-dependent thioredoxin reductase C (NTRC). We examined the redox-dependency of 5-aminolevulinic acid dehydratase (ALAD), which catalyzed the conjugation of two 5-aminolevulinic acid (ALA) molecules to porphobilinogen. ALAD interacted with TRX f, TRX m and NTRC in chloroplasts. Consequently, less ALAD protein accumulated in the trx f1, ntrc and trx f1/ntrc mutants compared to wild-type control resulting in decreased ALAD activity. In a polyacrylamide gel under non-reducing conditions, ALAD monomers turned out to be present in reduced and two oxidized forms. The reduced and oxidized forms of ALAD differed in their catalytic activity. The addition of TRX stimulated ALAD activity. From our results it was concluded that (i) deficiency of the reducing power mainly affected the in planta stability of ALAD; and (ii) the reduced form of ALAD displayed increased enzymatic activity. | - |
dc.language | eng | - |
dc.relation.ispartof | Antioxidants | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.subject | ALAD | - |
dc.subject | Chlorophyll | - |
dc.subject | Posttranslational modification | - |
dc.subject | Redox control | - |
dc.subject | Tetrapyrrole biosynthesis | - |
dc.subject | Thioredoxins | - |
dc.title | Towards initial indications for a thiol-based redox control of arabidopsis 5-aminolevulinic acid dehydratase | - |
dc.type | Article | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.3390/antiox7110152 | - |
dc.identifier.pmid | 30384439 | - |
dc.identifier.pmcid | PMC6262466 | - |
dc.identifier.scopus | eid_2-s2.0-85056341115 | - |
dc.identifier.volume | 7 | - |
dc.identifier.issue | 11 | - |
dc.identifier.spage | article no. 152 | - |
dc.identifier.epage | article no. 152 | - |
dc.identifier.eissn | 2076-3921 | - |
dc.identifier.isi | WOS:000451304600004 | - |