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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...

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Autores principales: Yuan, Ye, Liu, Zhiguo, Wang, Lili, Wang, Lixin, Chen, Shuangjiang, Niu, Yahong, Zhao, Xin, Liu, Ping, Liu, Mengjun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
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.
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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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