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Primary Structure of Sweet Potato Starch Phosphorylase Deduced from its cDNA Sequence
Open accessAbstract
Sweet potato (Ipomoea batatas) starch phosphorylase cDNA clones were isolated by screening an expression library prepared from the young root poly(A)(+) RNA successively with an antiserum, a monoclonal antibody, and a specific oligonucleotide probe. One cDNA clone had 3292 nucleotide residues in which was contained an open reading frame coding for 955 amino acids. This sequence was compared with those of potato (916 residues plus 50-residue putative transit peptide) and rabbit muscle (841 residues) phosphorylases. The sweet potato phosphorylase has an overall structural feature highly homologous to that reported for potato phosphorylase, in conformity with the finding that they belong to the same class of plant phosphorylase. High divergencies of the two enzymes are found in the about 70 residue N-termini each including a putative transit peptide, and the midchain 78 residue insert typical of type I plant phosphorylase. We consider that the very high dissimilarity found in the midchain inserts is related to the difference in proteolytic lability of the two plant phosphorylases. Some structural features of the cDNA clone were also discussed.
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“In sweet potato, the key enzymes involved in starch biosynthesis, including ADP-glucose pyrophosphorylase (AGPase, EC 2.7.7.27), granule-bound starch synthases (GBSS, EC 2.4.1.21), isoamylase (ISA, EC 3.2.1.68), starch-branching enzyme (SBE, EC 2.4.1.18), starch phosphorylase (SP, EC 2.4.1.1), and soluble starch synthase (SSS, EC 2.4.1.21), and their associated genes have been isolated and studied”
From Comparative Transcriptome Analysis Reveals Critical Function of Sucrose Metabolism Related-Enzymes in Starch Accumulation in the Storage Root of Sweet Potato (2017) · cites this paper as Lin et al., 1991
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Sonnewald, U., Basner, A., Greve, B., et al. (1995) · Plant Molecular Biology · doi:10.1007/bf00019322 · Cited by 94
Zhang, K., Wu, Z., Tang, D., Luo, K., Lu, H., Liu, Y., Dong, J., Wang, X., Lv, C., Wang, J., et al. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.00914 · Cited by 88
“…starch phosphorylase (SP, EC 2.4.1.1), and soluble starch synthase (SSS, EC 2.4.1.21), and their associated genes have been isolated and studied (Lin et al., 1991; Bae and Liu, 1997; Harn et al., 2000; Lee et al., 2000; Kim et al., 2005; Hamada et al., 2006; Ahn et al., 2010; Takahata et al.,…”
BackgroundInfluentialMcCool, B. A., Plonk, S. G., Martin, P., et al. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54089-8 · Cited by 81
Identification of the Maize Amyloplast Stromal 112-kD Protein as a Plastidic Starch Phosphorylase,
Yu, Y., Mu, H. H., Wasserman, B. P., et al. (2001) · PLANT PHYSIOLOGY · doi:10.1104/pp.125.1.351 · Cited by 70
“The three peptides of the 112-kD protein also aligned closely with sequences from the plastidic SP enzymes from potato leaf (Sonnewald et al., 1995), sweet potato (Lin et al., 1991), and spinach leaf (Duwenig et al., 1997a).”
BackgroundChen, H., Chang, S., Wu, C., et al. (2002) · Physiologia Plantarum · doi:10.1034/j.1399-3054.2002.1140402.x · Cited by 58
“Lin et al. (1991) deduced the primary structure of sweet potato L-SP from its cDNA sequence.”
BackgroundMethodResultInfluentialAlbrecht, T., Koch, A., Lode, A., et al. (2001) · Planta · doi:10.1007/s004250100525 · Cited by 52
Shoaib, N., Liu, L., Ali, A., Mughal, N., Yu, G., & Huang, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910450 · Cited by 44
“1) [14,78], orange (Citrus clementina; NW_0062622139.”
The plastidial starch phosphorylase from rice endosperm: catalytic properties at low temperature
Hwang, S., Singh, S., Cakir, B., et al. (2016) · Planta · doi:10.1007/s00425-015-2461-7 · Cited by 41
Young, G., Chen, H., Lin, C., et al. (2005) · Planta · doi:10.1007/s00425-005-0103-1 · Cited by 36
“M64362) is a cDNA clone of 3,292 nucleotide residues containing an open reading frame encoding for the 955 amino acids of L-SP from sweet potato roots (Lin et al. 1991).”
Self-citationDuwenig, E., Steup, M., & Koßmann, J. (1997) · Planta · doi:10.1007/s00050171 · Cited by 31
“…isolated from several plant species, namely potato (Brisson et al. 1989; Nakano et al. 1989; Mori et al. 1991; Sonnewald et al. 1995), sweet potato (Lin et al. 1990) and faba bean (Buchner et al. 1996), as well as from animals (rabbit: Titani et al. 1977) and bacteria (E. coli: Palm et al. 1985;…”
BackgroundResultInfluentialBüchner, P., Borisjuk, L., & Wobus, U. (1996) · Planta · doi:10.1007/bf00196882 · Cited by 31
Amylolytic Activity in Germinating Sweetpotato (Ipomoea batatas L.) Roots
Hagenimana, V., SIMARD, R. E., & Vézina, L. (1994) · Journal of the American Society for Horticultural Science · doi:10.21273/jashs.119.2.313 · Cited by 29
“…Ariki and Fukui (1975), who fou that sweetpotato starch phosphorylase had a similar mole structure and similar properties to the white potato enzyme, with Lin et al. (1991), who studied the homology between coding sequences of starch phosphorylase from potato (Solanum tuberosum) and sweetpotato.”
BackgroundThe Gene Structure of Starch Phosphorylase from Sweet Potato
Lin, C., Lin, M. T., Chou, H., et al. (1995) · PLANT PHYSIOLOGY · doi:10.1104/pp.107.1.277 · Cited by 23
“We have cloned and sequenced a cDNA encoding this L-type isozyme (Lin et al., 1991).”
BackgroundMethodSelf-citationDiscovery and Biotechnological Exploitation of Glycoside-Phosphorylases
Li, A., Benkoulouche, M., Ladevèze, S., Durand, J., Cioci, G., Laville, É., & Potocki-Véronèse, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063043 · Cited by 18
Lin, C., Yeh, K., Kao, M., et al. (1993) · Plant Molecular Biology · doi:10.1007/bf00021547 · Cited by 19
“The poly(A) + RNAs were isolated according to the oligo-(dT) affinity method [4] and then ligated with 2gtl0.”
MethodSelf-citationStarch phosphorylase: Biochemical and biotechnological perspectives
Tiwari, R. (2012) · Biotechnology and Molecular Biology Reviews · doi:10.5897/bmbr12.004 · Cited by 10
Slugina, M. A., Meleshin, A. A., Kochieva, E. Z., et al. (2019) · American Journal of Potato Research · doi:10.1007/s12230-019-09758-z · Cited by 9
Mizuno, S., Kamiyoshihara, Y., Shiba, H., et al. (2018) · Physiologia Plantarum · doi:10.1111/ppl.12886 · Cited by 9
The Identification of Starch Phosphorylase in the Developing Mungbean (Vigna radiata L.)
Ko, Y., Chang, J.-Y., Lee, Y.-T., et al. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf050193f · Cited by 8
Yu, S., Gómez‐Pinchetti, J. L., Garcia-Reina, G., et al. (1993) · Physiologia Plantarum · doi:10.1111/j.1399-3054.1993.tb01780.x · Cited by 5
Tanizawa, K., Mori, H., Tagaya, M., et al. (1994) · doi:10.1002/9783527615971.ch6 · Cited by 4
Yu, Y. (2002) · CRC Press eBooks · doi:10.1201/9780203910450.ch45
Discovery of new glycoside-phosphorylases for oligosaccharide synthesis
Li, A. (2020) · theses.fr (ABES) · doi:10.70675/9f013250zb7e3z456ezb9e4zc5ebee2e99ca
Metadata
- Authors
- Lin, C.-T., Yeh, K.-W., Lee, P.-D., & Su, J.-C.
- Affiliations
- National Taiwan University (TW)
- ORCID
- Yeh, Kai-Wun
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 1991-04-01
- Volume
- 95
- Issue
- 4
- Pages
- 1250-1253
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- PMC
- PMC1077680
- OpenAlex
- W2034151874
- Cited by
- 23
- References
- 0
- Citations by year
- 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 1 · 2012: 1
- FWCI
- 1.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- PLANT PHYSIOLOGY (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Glycogen Storage Diseases and Myoclonus
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant nutrient uptake and metabolism
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- Ipomoea batatas, cDNA sequence, primary structure, amino acid sequence homology, potato phosphorylase, transit peptide, monoclonal antibody screening, oligonucleotide probes
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