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Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity
Adenylyl cyclase (AC) is the key catalytic enzyme for the synthesis of 3′,5′-cyclic adenosine monophosphate. Various ACs have been identified in microorganisms and mammals, but studies on plant ACs are still limited. No AC in woody plants has been reported until now. Based on the information on HpAC...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9582125/ https://www.ncbi.nlm.nih.gov/pubmed/36275530 http://dx.doi.org/10.3389/fpls.2022.992488 |
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author | Yuan, Ye Liu, Zhiguo Wang, Lili Wang, Lixin Chen, Shuangjiang Niu, Yahong Zhao, Xin Liu, Ping Liu, Mengjun |
author_facet | Yuan, Ye Liu, Zhiguo Wang, Lili Wang, Lixin Chen, Shuangjiang Niu, Yahong Zhao, Xin Liu, Ping Liu, Mengjun |
author_sort | Yuan, Ye |
collection | PubMed |
description | Adenylyl cyclase (AC) is the key catalytic enzyme for the synthesis of 3′,5′-cyclic adenosine monophosphate. Various ACs have been identified in microorganisms and mammals, but studies on plant ACs are still limited. No AC in woody plants has been reported until now. Based on the information on HpAC1, three enzymes were screened out from the woody fruit tree apple, and two of them (MdTTM1 and MdTTM2) were verified and confirmed to display AC activity. Interestingly, in the apple genome, these two genes were annotated as triphosphate tunnel metalloenzymes (TTMs) which were widely found in three superkingdoms of life with multiple substrate specificities and enzymatic activities, especially triphosphate hydrolase. In addition, the predicted structures of these two proteins were parallel, especially of the catalytic tunnel, including conserved domains, motifs, and folded structures. Their tertiary structures exhibited classic TTM properties, like the characteristic EXEXK motif and β-stranded anti-parallel tunnel capable of coordinating divalent cations. Moreover, MdTTM2 and HpAC1 displayed powerful hydrolase activity to triphosphate and restricted AC activity. All of these findings showed that MdTTMs had hydrolysis and AC activity, which could provide new solid evidence for AC distribution in woody plants as well as insights into the relationship between ACs and TTMs. |
format | Online Article Text |
id | pubmed-9582125 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-95821252022-10-21 Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity Yuan, Ye Liu, Zhiguo Wang, Lili Wang, Lixin Chen, Shuangjiang Niu, Yahong Zhao, Xin Liu, Ping Liu, Mengjun Front Plant Sci Plant Science Adenylyl cyclase (AC) is the key catalytic enzyme for the synthesis of 3′,5′-cyclic adenosine monophosphate. Various ACs have been identified in microorganisms and mammals, but studies on plant ACs are still limited. No AC in woody plants has been reported until now. Based on the information on HpAC1, three enzymes were screened out from the woody fruit tree apple, and two of them (MdTTM1 and MdTTM2) were verified and confirmed to display AC activity. Interestingly, in the apple genome, these two genes were annotated as triphosphate tunnel metalloenzymes (TTMs) which were widely found in three superkingdoms of life with multiple substrate specificities and enzymatic activities, especially triphosphate hydrolase. In addition, the predicted structures of these two proteins were parallel, especially of the catalytic tunnel, including conserved domains, motifs, and folded structures. Their tertiary structures exhibited classic TTM properties, like the characteristic EXEXK motif and β-stranded anti-parallel tunnel capable of coordinating divalent cations. Moreover, MdTTM2 and HpAC1 displayed powerful hydrolase activity to triphosphate and restricted AC activity. All of these findings showed that MdTTMs had hydrolysis and AC activity, which could provide new solid evidence for AC distribution in woody plants as well as insights into the relationship between ACs and TTMs. Frontiers Media S.A. 2022-10-06 /pmc/articles/PMC9582125/ /pubmed/36275530 http://dx.doi.org/10.3389/fpls.2022.992488 Text en Copyright © 2022 Yuan, Liu, Wang, Wang, Chen, Niu, Zhao, Liu and Liu https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Yuan, Ye Liu, Zhiguo Wang, Lili Wang, Lixin Chen, Shuangjiang Niu, Yahong Zhao, Xin Liu, Ping Liu, Mengjun Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity |
title | Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity |
title_full | Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity |
title_fullStr | Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity |
title_full_unstemmed | Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity |
title_short | Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity |
title_sort | two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9582125/ https://www.ncbi.nlm.nih.gov/pubmed/36275530 http://dx.doi.org/10.3389/fpls.2022.992488 |
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