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Sedoheptulose-bisphosphatase

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sedoheptulose-bisphosphatase
Crystallographic structure of sedoheptulose-bisphosphatase from Toxoplasma gondii [1]
Identifiers
EC no.3.1.3.37
CAS no.9055-32-7
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Sedoheptulose-bisphosphatase (also sedoheptulose-1,7-bisphosphatase or SBPase, EC number 3.1.3.37; systematic name sedoheptulose-1,7-bisphosphate 1-phosphohydrolase) is an enzyme that catalyzes the removal of a phosphate group from sedoheptulose 1,7-bisphosphate to produce sedoheptulose 7-phosphate. SBPase is an example of a phosphatase, or, more generally, a hydrolase. This enzyme participates in the Calvin cycle.

Structure

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SBPase is a homodimeric protein, meaning that it is made up of two identical subunits.[2] The size of this protein varies between species, but is about 92,000 Da (two 46,000 Da subunits) in cucumber plant leaves.[3] The key functional domain controlling SBPase function involves a disulfide bond between two cysteine residues.[4] These two cysteine residues, Cys52 and Cys57, appear to be located in a flexible loop between the two subunits of the homodimer,[5] near the active site of the enzyme. Reduction of this regulatory disulfide bond by thioredoxin incites a conformational change in the active site, activating the enzyme.[6] Additionally, SBPase requires the presence of magnesium (Mg2+) to be functionally active.[7] SBPase is bound to the stroma-facing side of the thylakoid membrane in the chloroplast in a plant. Some studies have suggested the SBPase may be part of a large (900 kDa) multi-enzyme complex along with a number of other photosynthetic enzymes.[8]

Regulation

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Reaction catalyzed by sedoheptulose-bisphosphatase

SBPase is involved in the regeneration of 5-carbon sugars during the Calvin cycle. Although SBPase has not been emphasized as an important control point in the Calvin cycle historically, it plays a large part in controlling the flux of carbon through the Calvin cycle.[9] Additionally, SBPase activity has been found to have a strong correlation with the amount of photosynthetic carbon fixation.[10] Like many Calvin cycle enzymes, SBPase is activated in the presence of light through a ferredoxin/thioredoxin system.[11] In the light reactions of photosynthesis, light energy powers the transport of electrons to eventually reduce ferredoxin. The enzyme ferredoxin-thioredoxin reductase uses reduced ferredoxin to reduce thioredoxin from the disulfide form to the dithiol. Finally, the reduced thioredoxin is used to reduced a cysteine-cysteine disulfide bond in SBPase to a dithiol, which converts the SBPase into its active form.[7]

This is an illustration of the regulation of SBPase by ferredoxin and thioredoxin.[9]

SBPase has additional levels of regulation beyond the ferredoxin/thioredoxin system. Mg2+ concentration has a significant impact on the activity of SBPase and the rate of the reactions it catalyzes.[12] SBPase is inhibited by acidic conditions (low pH). This is a large contributor to the overall inhibition of carbon fixation when the pH is low inside the stroma of the chloroplast.[13] Finally, SBPase is subject to negative feedback regulation by sedoheptulose-7-phosphate and inorganic phosphate, the products of the reaction it catalyzes.[14]

Evolutionary origin

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SBPase and FBPase (fructose-1,6-bisphosphatase, EC 3.1.3.11) are both phosphatases that catalyze similar during the Calvin cycle. The genes for SBPase and FBPase are related. Both genes are found in the nucleus in plants, and have bacterial ancestry.[15] SBPase is found across many species. In addition to being universally present in photosynthetic organism, SBPase is found in a number of evolutionarily-related, non-photosynthetic microorganisms. SBPase likely originated in red algae.[16]

Horticultural Relevance

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Carbonylation of a cysteine residue via hydroxyl radical, analogous to how SBPase is inactivated by ROS.

Moreso than other enzymes in the Calvin cycle, SBPase levels have a significant impact on plant growth, photosynthetic ability, and response to environmental stresses. Small decreases in SBPase activity result in decreased photosynthetic carbon fixation and reduced plant biomass.[17] Specifically, decreased SBPase levels result in stunted plant organ growth and development compared to wild-type plants,[18] and starch levels decrease linearly with decreases in SBPase activity, suggesting that SBPase activity is a limiting factor to carbon assimilation.[19] This sensitivity of plants to decreased SBPase activity is significant, as SBPase itself is sensitive to oxidative damage and inactivation from environmental stresses. SBPase contains several catalytically relevant cysteine residues that are vulnerable to irreversible oxidative carbonylation by reactive oxygen species (ROS),[20] particularly from hydroxyl radicals created during the production of hydrogen peroxide.[21] Carbonylation results in SBPase enzyme inactivation and subsequent growth retardation due to inhibition of carbon assimilation.[18] Oxidative carbonylation of SBPase can be induced by environmental pressures such as chilling, which causes an imbalance in metabolic processes leading to increased production of reactive oxygen species, particularly hydrogen peroxide.[21]  Notably, chilling inhibits SBPase and a related enzyme, fructose bisphosphatase, but does not affect other reductively activated Calvin cycle enzymes.[22]

The sensitivity of plants to synthetically reduced or inhibited SBPase levels provides an opportunity for crop engineering. There are significant indications that transgenic plants which overexpress SBPase may be useful in improving food production efficiency by producing crops that are more resilient to environmental stresses, as well as have earlier maturation and higher yield. Overexpression of SBPase in transgenic tomato plants provided resistance to chilling stress, with the transgenic plants maintaining higher SBPase activity, increased carbon dioxide fixation, reduced electrolyte leakage and increased carbohydrate accumulation relative to wild-type plants under the same chilling stress.[21] It is also likely that transgenic plants would be more resilient to osmotic stress caused by drought or salinity, as the activation of SBPase is shown to be inhibited in chloroplasts exposed to hypertonic conditions,[23] though this has not been directly tested. Overexpression of SBPase in transgenic tobacco plants resulted in enhanced photosynthetic efficiency and growth. Specifically, transgenic plants exhibited greater biomass and improved carbon dioxide fixation, as well as an increase in RuBisCO activity. The plants grew significantly faster and larger than wild-type plants, with increased sucrose and starch levels.[24]

References

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  1. ^ Minasov G, Ruan J, Wawrzak Z, Halavaty A, Shuvalova L, Harb OS, Ngo H, Anderson WF (2013). "1.85 Angstrom Crystal Structure of Putative Sedoheptulose-1,7 bisphosphatase from Toxoplasma gondii". doi:10.2210/pdb4ir8/pdb. {{cite journal}}: Cite journal requires |journal= (help)
  2. ^ Hino M, Nagatsu T, Kakumu S, Okuyama S, Yoshii Y, Nagatsu I (July 1975). "Glycylprolyl β-naphthylamidase activity in human serum". Clinica Chimica Acta; International Journal of Clinical Chemistry. 62 (1): 5–11. doi:10.1016/0009-8981(75)90273-9. PMID 1149281.
  3. ^ Wang M, Bi H, Liu P, Ai X (2011). "Molecular cloning and expression analysis of the gene encoding sedoheptulose-1, 7-bisphosphatase from Cucumis sativus". Scientia Horticulturae. 129 (3): 414–420. Bibcode:2011ScHor.129..414W. doi:10.1016/j.scienta.2011.04.010.
  4. ^ Anderson LE, Huppe HC, Li AD, Stevens FJ (September 1996). "Identification of a potential redox-sensitive interdomain disulfide in the sedoheptulose bisphosphatase of Chlamydomonas reinhardtii". The Plant Journal. 10 (3): 553–60. doi:10.1046/j.1365-313X.1996.10030553.x. PMID 8811868.
  5. ^ Dunford RP, Durrant MC, Catley MA, Dyer TA (1998-12-01). "Location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphosphatase indicates that its allosteric regulation is similar but not identical to that of fructose-1,6-bisphosphatase". Photosynthesis Research. 58 (3): 221–230. doi:10.1023/A:1006178826976. ISSN 1573-5079. S2CID 25845982.
  6. ^ Raines CA, Harrison EP, Ölçer H, Lloyd JC (2000). "Investigating the role of the thiol-regulated enzyme sedoheptulose-1,7-bisphosphatase in the control of photosynthesis". Physiologia Plantarum. 110 (3): 303–308. doi:10.1111/j.1399-3054.2000.1100303.x. ISSN 1399-3054.
  7. ^ a b Nakamura Y, Tada T, Wada K, Kinoshita T, Tamoi M, Shigeoka S, Nishimura K (March 2001). "Purification, crystallization and preliminary X-ray diffraction analysis of the fructose-1,6-/sedoheptulose-1,7-bisphosphatase of Synechococcus PCC 7942". Acta Crystallographica. Section D, Biological Crystallography. 57 (Pt 3): 454–6. doi:10.1107/S0907444901002177. PMID 11223530.
  8. ^ Suss KH, Arkona C, Manteuffel R, Adler K (June 1993). "Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ". Proceedings of the National Academy of Sciences of the United States of America. 90 (12): 5514–8. Bibcode:1993PNAS...90.5514S. doi:10.1073/pnas.90.12.5514. PMC 46751. PMID 11607406.
  9. ^ a b Raines CA, Lloyd JC, Dyer TA (1999). "New insights into the structure and function of sedoheptulose-1,7-bisphosphatase; an important but neglected Calvin cycle enzyme". Journal of Experimental Botany. 50 (330): 1–8. doi:10.1093/jxb/50.330.1.
  10. ^ Olçer H, Lloyd JC, Raines CA (February 2001). "Photosynthetic capacity is differentially affected by reductions in sedoheptulose-1,7-bisphosphatase activity during leaf development in transgenic tobacco plants". Plant Physiology. 125 (2): 982–9. doi:10.1104/pp.125.2.982. PMC 64898. PMID 11161054.
  11. ^ Breazeale VD, Buchanan BB, Wolosiuk RA (May 1978). "Chloroplast Sedoheptulose 1,7 Bisphosphatase: Evidence for Regulation by the Ferridoxin/Thioredoxin System". Zeitschrift für Naturforschung C. 33 (7–8): 521–528. doi:10.1515/znc-1978-7-812.
  12. ^ Woodrow IE, Walker DA (July 1982). "Activation of wheat chloroplast sedoheptulose bisphosphatase: a continuous spectrophotometric assay". Archives of Biochemistry and Biophysics. 216 (2): 416–22. doi:10.1016/0003-9861(82)90230-2. PMID 6287934.
  13. ^ Purczeld P, Chon CJ, Portis AR, Heldt HW, Heber U (March 1978). "The mechanism of the control of carbon fixation by the pH in the chloroplast stroma. Studies with nitrite-mediated proton transfer across the envelope". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 501 (3): 488–98. doi:10.1016/0005-2728(78)90116-0. PMID 24470.
  14. ^ Schimkat D, Heineke D, Heldt HW (April 1990). "Regulation of sedoheptulose-1,7-bisphosphatase by sedoheptulose-7-phosphate and glycerate, and of fructose-1,6-bisphosphatase by glycerate in spinach chloroplasts". Planta. 181 (1): 97–103. doi:10.1007/BF00202330. PMID 24196680. S2CID 7395500.
  15. ^ Martin W, Mustafa AZ, Henze K, Schnarrenberger C (November 1996). "Higher-plant chloroplast and cytosolic fructose-1,6-bisphosphatase isoenzymes: origins via duplication rather than prokaryote-eukaryote divergence". Plant Molecular Biology. 32 (3): 485–91. doi:10.1007/BF00019100. PMID 8980497. S2CID 21599476.
  16. ^ Teich R, Zauner S, Baurain D, Brinkmann H, Petersen J (July 2007). "Origin and distribution of Calvin cycle fructose and sedoheptulose bisphosphatases in plantae and complex algae: a single secondary origin of complex red plastids and subsequent propagation via tertiary endosymbioses". Protist. 158 (3): 263–76. doi:10.1016/j.protis.2006.12.004. hdl:2268/71085. PMID 17368985.
  17. ^ Raines CA (2003-01-01). "The Calvin cycle revisited". Photosynthesis Research. 75 (1): 1–10. doi:10.1023/A:1022421515027. ISSN 1573-5079. PMID 16245089. S2CID 21786477.
  18. ^ a b Liu XL, Yu HD, Guan Y, Li JK, Guo FQ (September 2012). "Carbonylation and loss-of-function analyses of SBPase reveal its metabolic interface role in oxidative stress, carbon assimilation, and multiple aspects of growth and development in Arabidopsis". Molecular Plant. 5 (5): 1082–99. doi:10.1093/mp/sss012. PMID 22402261.
  19. ^ Harrison EP, Willingham NM, Lloyd JC, Raines CA (1997-12-01). "Reduced sedoheptulose-1,7-bisphosphatase levels in transgenic tobacco lead to decreased photosynthetic capacity and altered carbohydrate accumulation". Planta. 204 (1): 27–36. Bibcode:1997Plant.204...27H. doi:10.1007/s004250050226. ISSN 1432-2048. S2CID 24243453.
  20. ^ Møller IM, Jensen PE, Hansson A (June 2007). "Oxidative modifications to cellular components in plants". Annual Review of Plant Biology. 58 (1): 459–81. doi:10.1146/annurev.arplant.58.032806.103946. PMID 17288534.
  21. ^ a b c Ding F, Wang M, Zhang S (2017-01-05). "Overexpression of a Calvin cycle enzyme SBPase improves tolerance to chilling-induced oxidative stress in tomato plants". Scientia Horticulturae. 214: 27–33. Bibcode:2017ScHor.214...27D. doi:10.1016/j.scienta.2016.11.010. ISSN 0304-4238.
  22. ^ Hutchison RS, Groom Q, Ort DR (June 2000). "Differential effects of chilling-induced photooxidation on the redox regulation of photosynthetic enzymes". Biochemistry. 39 (22): 6679–88. doi:10.1021/bi0001978. PMID 10828986.
  23. ^ Boag S, Portis AR (January 1984). "Inhibited light activation of fructose and sedoheptulose bisphosphatase in spinach chloroplasts exposed to osmotic stress". Planta. 160 (1): 33–40. Bibcode:1984Plant.160...33B. doi:10.1007/BF00392463. PMID 24258369. S2CID 9480244.
  24. ^ Miyagawa Y, Tamoi M, Shigeoka S (October 2001). "Overexpression of a cyanobacterial fructose-1,6-/sedoheptulose-1,7-bisphosphatase in tobacco enhances photosynthesis and growth". Nature Biotechnology. 19 (10): 965–9. doi:10.1038/nbt1001-965. PMID 11581664. S2CID 7288017.

Further reading

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