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Increased activity of sugarcane sucrose‐phosphate synthase in transgenic tomato in response to N‐terminal truncation

Indonesian Journal of Biotechnology · Vol. 27 No. 1 (2022) · hlm. 43–50

DOI
10.22146/ijbiotech.69337
ISSN
2089-2241, 0853-8654
Terbit
2022-03-29
Penerbit
Universitas Gadjah Mada
Bahasa
eng
Lisensi
creativecommons.org/licenses/by-sa/4.0

Abstrak

Sucrose‐phosphate synthase (SPS) is a key enzyme catalyzing the formation of sucrose‐6‐phosphate through the transfer of uridine‐diphosphate glucose (UDP‐G) as a donor to fructose‐6‐phosphate (F6P) as an acceptor. Plant SPS consists of three main domains: N‐terminal, glycosyltransferase, and C‐terminal domains. Among these, the N‐terminal domain is involved in regulating the allosteric activator glucose‐6‐phosphate (G6P). This study was directed toward determining the regulation and characterization of N‐terminal truncated SPS in transgenic tomato. In this study, the N‐terminal truncated mutant of sugarcane SPS (ΔN‐SoSPS1) and full‐length sugarcane SPS (FL‐SoSPS1) were expressed into tomato plants to verify the functional role and importance of the N‐terminal domain in plant SPS. Overexpression of ΔN‐SoSPS1 led to an up to 3‐fold increase in the specific activity of SPS compared to non‐transformant plants (WT), while the specific activity of ΔN‐SoSPS1 was higher than FL‐SoSPS1 in transgenic tomato plants. Unlike WT and FL‐SoSPS1, the ΔN‐SoSPS1 mutant was not allosterically regulated by G6P. These results indicated that deletion of the N‐terminal domain promotes the loss of allosteric activation by G6P and increases binding affinity between enzyme and substrate.

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Wahyu Indra Duwi FanataAfiliasi tidak diketahui4
Didik Pudji RestantoAfiliasi tidak diketahui3
Tri HandoyoAfiliasi tidak diketahui2
Yusuf Dary AhnafAfiliasi tidak diketahui2
IryonoAfiliasi tidak diketahui2
Syafira Fatihatul HusnaAfiliasi tidak diketahui2
Popy Hartatie HardjoAfiliasi tidak diketahui1
Mohammad Candra PrayogaAfiliasi tidak diketahui1
Sigit SoeparjonoAfiliasi tidak diketahui1
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Intan Ria NelianaAfiliasi tidak diketahui1
Cassidy MagnonAfiliasi tidak diketahui1
Numalasari NumalasariAfiliasi tidak diketahui1
Falin Fatimatus ShahroAfiliasi tidak diketahui1
Fakhriyah Nur KhalilahAfiliasi tidak diketahui1
Hayati Aulia MaharaniAfiliasi tidak diketahui1
Kyung-Min KimAfiliasi tidak diketahui1
Mohammad Nur KhozinAfiliasi tidak diketahui1
Mohammad UbaidillahAfiliasi tidak diketahui1
Nabila Nur Aisyah Al AyyubiAfiliasi tidak diketahui1
Rendryana Aulia Nur KhofifaAfiliasi tidak diketahui1
Slameto SlametoAfiliasi tidak diketahui1
Nur BasukiAfiliasi tidak diketahui1
Liliek SulistyowatiAfiliasi tidak diketahui1
Mohammad Nur KhozinAfiliasi tidak diketahui1
HARDIAN SUSILO ADDYAfiliasi tidak diketahui1
Weny Nailul HidayatiAfiliasi tidak diketahui1
Retnosari ApriastiAfiliasi tidak diketahui1
Sholeh AviviUniversitas Jember1
Galang Rizki RamadhanAfiliasi tidak diketahui1

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Sumber metadata: OAI-PMH (metadata jurnal) https://jurnal.ugm.ac.id/ijbiotech/oai, pertama di-harvest 8 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (oai_dc) 
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	<dc:title xml:lang="en-US">Increased activity of sugarcane sucrose‐phosphate synthase in transgenic tomato in response to N‐terminal truncation</dc:title>
	<dc:creator>Afidah, Siti Nurul</dc:creator>
	<dc:creator>Agustien, Inyana Dwi</dc:creator>
	<dc:creator>Dewanti, Parawita</dc:creator>
	<dc:creator>Sugiharto, Bambang</dc:creator>
	<dc:subject xml:lang="en-US">sucrose‐phosphate synthase; glucose‐6‐phosphate; sucrose synthesis; allosteric regulation; N‐terminal domain</dc:subject>
	<dc:description xml:lang="en-US">Sucrose‐phosphate synthase (SPS) is a key enzyme catalyzing the formation of sucrose‐6‐phosphate through the transfer of uridine‐diphosphate glucose (UDP‐G) as a donor to fructose‐6‐phosphate (F6P) as an acceptor. Plant SPS consists of three main domains: N‐terminal, glycosyltransferase, and C‐terminal domains. Among these, the N‐terminal domain is involved in regulating the allosteric activator glucose‐6‐phosphate (G6P). This study was directed toward determining the regulation and characterization of N‐terminal truncated SPS in transgenic tomato. In this study, the N‐terminal truncated mutant of sugarcane SPS (ΔN‐SoSPS1) and full‐length sugarcane SPS (FL‐SoSPS1) were expressed into tomato plants to verify the functional role and importance of the N‐terminal domain in plant SPS. Overexpression of ΔN‐SoSPS1 led to an up to 3‐fold increase in the specific activity of SPS compared to non‐transformant plants (WT), while the specific activity of ΔN‐SoSPS1 was higher than FL‐SoSPS1 in transgenic tomato plants. Unlike WT and FL‐SoSPS1, the ΔN‐SoSPS1 mutant was not allosterically regulated by G6P. These results indicated that deletion of the N‐terminal domain promotes the loss of allosteric activation by G6P and increases binding affinity between enzyme and substrate.</dc:description>
	<dc:publisher xml:lang="en-US">Universitas Gadjah Mada</dc:publisher>
	<dc:contributor xml:lang="en-US"></dc:contributor>
	<dc:date>2022-03-29</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:type xml:lang="en-US">Original Research Articles</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.ugm.ac.id/ijbiotech/article/view/69337</dc:identifier>
	<dc:identifier>10.22146/ijbiotech.69337</dc:identifier>
	<dc:source xml:lang="en-US">Indonesian Journal of Biotechnology; Vol 27, No 1 (2022); 43-50</dc:source>
	<dc:source>2089-2241</dc:source>
	<dc:source>0853-8654</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/view/69337/33387</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20725</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20726</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20727</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20728</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20729</dc:relation>
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	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20731</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20732</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20733</dc:relation>
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	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/69337/20735</dc:relation>
	<dc:rights xml:lang="en-US">Copyright (c) 2022 The Author(s)</dc:rights>
	<dc:rights xml:lang="en-US">http://creativecommons.org/licenses/by-sa/4.0</dc:rights>
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