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R UBISCO : Structure, Regulatory Interactions, and Possibilities for a Better Enzyme
Abstract
Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) catalyzes the first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation. The enzyme is notoriously inefficient as a catalyst for the carboxylation of RuBP and is subject to competitive inhibition by O2, inactivation by loss of carbamylation, and dead-end inhibition by RuBP. These inadequacies make Rubisco rate limiting for photosynthesis and an obvious target for increasing agricultural productivity. Resolution of X-ray crystal structures and detailed analysis of divergent, mutant, and hybrid enzymes have increased our insight into the structure/function relationships of Rubisco. The interactions and associations relatively far from the Rubisco active site, including regulatory interactions with Rubisco activase, may present new approaches and strategies for understanding and ultimately improving this complex enzyme.
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“The activity of Rubisco is regulated by Rca, which facilitates the dissociation of inhibitory sugar phosphates from the active site of Rubisco in an ATP-dependent manner (Spreitzer and Salvucci, 2002).”
From Rubisco and Rubisco Activase Play an Important Role in the Biochemical Limitations of Photosynthesis in Rice, Wheat, and Maize under High Temperature and Water Deficit (2017) · cites this paper as Spreitzer and Salvucci, 2002
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CO2 CONCENTRATING MECHANISMS IN PHOTOSYNTHETIC MICROORGANISMS
Kaplan, A., & Reinhold, L. (1999) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.50.1.539 · Cited by 693
Mechanism of Rubisco: the carbamate as general base
Cleland, W. W., Andrews, T. J., Gutteridge, S., Hartman, F. C., & Lorimer, G. H. (1998) · Chemical Reviews · doi:10.1021/cr970010r · Cited by 430
Purification and species distribution of Rubisco activase.
Salvucci, M. E., Werneke, J. M., Ogren, W. L., & Portis, A. R. (1987) · Plant Physiology · doi:10.1104/pp.84.3.930 · Cited by 152
Self-citation
Research works printed but not linked: 158
- 10.1007/BF00042971 · DOI
- 10.1016/0304-4165(79)90319-2 · DOI
- 10.1006/jmbi.1996.0310 · DOI
- 10.1038/337229a0 · DOI
- Andrews TJ, 1988, J. Biol. Chem., 263, 12213, 10.1016/S0021-9258(18)37741-X · DOI
- 10.1038/nsb0196-3 · DOI
- Andrews TJ, 1985, J. Biol. Chem., 260, 4632, 10.1016/S0021-9258(18)89117-7 · DOI
- 10.1002/j.1460-2075.1989.tb03594.x · DOI
- 10.1042/bj3360387 · DOI
- 10.1093/nar/28.1.235 · DOI · Paper page
- 10.1007/978-94-009-0383-8_142 · DOI
- 10.1074/jbc.270.20.11741 · DOI
- 10.1073/pnas.85.13.4696 · DOI
- Chen Z, 1989, J. Biol. Chem., 264, 3051, 10.1016/S0021-9258(18)94027-5 · DOI
- 10.1111/j.1399-3054.1991.tb02474.x · DOI
- 10.1007/BF00028792 · DOI
- 10.1021/bi00100a017 · DOI
- 10.1016/0022-2836(92)90408-C · DOI
- 10.1006/bbrc.1997.6318 · DOI
- 10.1093/protein/11.6.457 · DOI
- 10.1073/pnas.90.2.363 · DOI
- 10.1073/pnas.94.15.7791 · DOI
- 10.1007/BF00042362 · DOI
- 10.1073/pnas.230451497 · DOI · Paper page
- 10.1104/pp.114.2.439 · DOI
- 10.1021/bi00059a009 · DOI
- 10.1146/annurev.pp.40.060189.002215 · DOI
- 10.1093/jxb/44.1.1 · DOI
- 10.1073/pnas.260503997 · DOI
- 10.1074/jbc.M002321200 · DOI
- 10.1006/jmbi.2000.3724 · DOI
- 10.1104/pp.113.2.575 · DOI
- 10.1016/0014-5793(90)80066-R · DOI
- 10.1016/0968-0004(79)90212-3 · DOI
- 10.1006/abbi.1996.0052 · DOI
- 10.1023/A:1006133212261 · DOI
- 10.1128/jb.173.6.2099-2108.1991 · DOI
- 10.1104/pp.116.2.539 · DOI
- Flachmann R, 1992, J. Biol. Chem., 267, 10576, 10.1016/S0021-9258(19)50055-2 · DOI
- 10.1104/pp.114.1.131 · DOI
- 10.1111/j.1432-1033.1987.tb13409.x · DOI
- 10.1104/pp.116.2.695 · DOI
- Gutteridge S, 1991, J. Biol. Chem., 266, 7359, 10.1016/S0021-9258(20)89454-X · DOI
- Gutteridge S, 1988, Plant Physiol. Biochem., 26, 675
- Gutteridge S, 1993, J. Biol. Chem., 268, 7818, 10.1016/S0021-9258(18)53031-3 · DOI
- 10.1006/jmbi.1999.2701 · DOI
- 10.1073/pnas.081610398 · DOI
- 10.1021/bi00184a026 · DOI
- 10.1021/bi962184t · DOI
- 10.1002/pro.5560070322 · DOI
- 10.1021/bi00035a039 · DOI
- 10.1146/annurev.bi.63.070194.001213 · DOI
- 10.1074/jbc.272.17.11114 · DOI
- 10.1104/pp.98.1.294 · DOI
- Jordan DB, 1983, J. Biol. Chem., 258, 13752, 10.1016/S0021-9258(17)43982-2 · DOI
- 10.1038/291513a0 · DOI
- 10.1007/BF00398720 · DOI
- 10.1104/pp.123.3.1077 · DOI
- 10.1104/pp.119.1.133 · DOI
- 10.1071/PP9940449 · DOI
- 10.2307/2446015 · DOI
- 10.1093/jxb/46.special_issue.1245 · DOI
- 10.1073/pnas.93.24.13689 · DOI
- 10.1021/bi981598e · DOI
- 10.1007/BF00029934 · DOI
- 10.1016/S0022-2836(05)80100-7 · DOI
- 10.1023/A:1005967106993 · DOI
- 10.1104/pp.54.5.678 · DOI
- Larimer FW, 1994, J. Biol. Chem., 269, 11114, 10.1016/S0021-9258(19)78099-5 · DOI
- 10.1021/bi00014a005 · DOI
- 10.1074/jbc.272.27.17033 · DOI
- 10.1016/0003-9861(91)90133-4 · DOI
- 10.1002/pro.5560020709 · DOI
- 10.1007/BF00027109 · DOI
- 10.1023/A:1006251808625 · DOI
- 10.1104/pp.114.2.605 · DOI
- Lorimer GH, 1988, J. Biol. Chem., 263, 6468, 10.1016/S0021-9258(18)68663-6 · DOI
- 10.1021/bi00564a027 · DOI
- 10.1046/j.1432-1327.1998.2530476.x · DOI
- 10.1006/jmbi.1999.3145 · DOI
- 10.1126/science.283.5400.314 · DOI
- 10.1104/pp.102.4.1119 · DOI
- 10.1146/annurev.arplant.52.1.297 · DOI · Paper page
- 10.1016/0003-9861(92)90278-5 · DOI
- 10.1074/jbc.272.9.5445 · DOI
- 10.1074/jbc.274.38.26789 · DOI
- 10.1126/science.7777861 · DOI
- Neuwald AF, 1999, Genome Res., 9, 27, 10.1101/gr.9.1.27 · DOI
- Newman J, 1993, J. Biol. Chem., 268, 25876, 10.1016/S0021-9258(19)74469-X · DOI
- 10.1146/annurev.pp.35.060184.002215 · DOI
- 10.1074/jbc.M004580200 · DOI
- 10.1007/BF00201937 · DOI
- Pierce J, 1986, J. Biol. Chem., 261, 10248, 10.1016/S0021-9258(18)67516-7 · DOI
- 10.1073/pnas.86.15.5753 · DOI
- 10.1093/jxb/46.special_issue.1285 · DOI
- 10.1128/jb.175.10.2871-2879.1993 · DOI
- Qian Y, 1998, J. Bacteriol., 180, 4644, 10.1128/JB.180.17.4644-4649.1998 · DOI
- 10.1006/abbi.1997.0438 · DOI
- 10.1021/bi00139a018 · DOI
- 10.1006/abbi.1994.1301 · DOI
- 10.1104/pp.94.4.1837 · DOI
- 10.1016/0014-5793(88)80473-3 · DOI
- 10.1016/0003-9861(89)90568-7 · DOI
- 10.1104/pp.90.3.968 · DOI
- 10.1007/0-306-48204-5 · DOI
- Romanova AK, 1997, Biochem. Mol. Biol. Int., 42, 299
- Roy H, Andrews TJ. 2000. Rubisco: assembly and mechanism. In Photosynthesis: Physiology and Metabolism , ed. RC Leegood, TD Sharkey, S von Caemmerer, pp. 53–83. Dordrecht: Kluwer · DOI
- Rundle SJ, 1991, J. Biol. Chem., 266, 4677, 10.1016/S0021-9258(19)67702-1 · DOI
- 10.1104/pp.122.2.491 · DOI
- 10.1016/0003-9861(92)90467-B · DOI
- 10.1104/pp.85.1.66 · DOI
- 10.1007/BF00017748 · DOI
- 10.1104/pp.127.3.1053 · DOI
- 10.1104/pp.80.3.655 · DOI
- 10.1073/pnas.031568098 · DOI
- 10.1002/pro.5560020708 · DOI
- 10.1007/BF00035005 · DOI
- Shen JB, 1991, J. Biol. Chem., 266, 8963, 10.1016/S0021-9258(18)31538-2 · DOI
- 10.1007/BF00021801 · DOI
- Soper TS, 1992, J. Biol. Chem., 267, 8452, 10.1016/S0021-9258(18)42465-9 · DOI
- Spalding MH. 1998. CO 2 concentrating mechanism. See Ref.106A, pp. 529–47
- 10.1146/annurev.pp.44.060193.002211 · DOI
- Spreitzer RJ. 1998. Genetic engineering of Rubisco. See Ref.106A, pp. 515–27 · DOI
- 10.1023/A:1006240202051 · DOI
- 10.1021/bi002943e · DOI
- 10.1104/pp.109.2.681 · DOI
- 10.1104/pp.85.1.152 · DOI
- 10.1074/jbc.274.22.15655 · DOI
- Suzuki K, 1995, Plant Cell Physiol., 36, 95
- 10.1023/A:1006211417981 · DOI
- 10.1038/nsb0196-95 · DOI
- 10.1021/bi962818w · DOI
- 10.1006/jmbi.1996.0738 · DOI
- 10.1074/jbc.M107765200 · DOI
- 10.1074/jbc.271.51.32894 · DOI
- 10.1021/bi00183a014 · DOI
- 10.1007/s004250050607 · DOI
- 10.1006/bbrc.1997.6497 · DOI
- 10.1093/oxfordjournals.jbchem.a022791 · DOI
- 10.1021/bi9604901 · DOI
- 10.1021/bi972566e · DOI
- 10.1126/science.7913555 · DOI
- 10.1104/pp.113.2.469 · DOI
- 10.1104/pp.99.4.1348 · DOI
- 10.1016/0167-4838(93)90061-U · DOI
- 10.1104/pp.100.4.1858 · DOI
- 10.1073/pnas.86.4.1198 · DOI
- 10.1104/pp.87.4.917 · DOI
- 10.1105/tpc.1.8.815 · DOI
- 10.1071/PP97131 · DOI
- 10.1105/tpc.13.1.193 · DOI
- 10.1104/pp.121.2.579 · DOI
- 10.1111/j.1432-1033.1992.tb16710.x · DOI
- 10.1073/pnas.96.16.9438 · DOI · Paper page
- 10.1093/oxfordjournals.jbchem.a022765 · DOI
- 10.1104/pp.97.4.1348 · DOI
- Zhu G, 1994, J. Biol. Chem., 269, 3952, 10.1016/S0021-9258(17)41726-1 · DOI
- 10.1074/jbc.271.31.18494 · DOI
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Metadata
- Authors
- Spreitzer, R. J., & Salvucci, M. E.
- Affiliations
- University of Nebraska–Lincoln (US)
- Agricultural Research Service (US)
- Venue
- Annual Review of Plant Biology
- Publisher
- Annual Reviews
- Published
- 2002-06
- Volume
- 53
- Issue
- 1
- Pages
- 449-475
- ISSN
- 1543-5008 (ISSN-L)
- 1545-2123
- OpenAlex
- W2125073348
- Cited by
- 876
- References
- 3
- Citations by year
- 2026: 20 · 2025: 33 · 2024: 26 · 2023: 36 · 2022: 32 · 2021: 31 · 2020: 45 · 2019: 43 · 2018: 45 · 2017: 45 · 2016: 53 · 2015: 40 · 2014: 45 · 2013: 48 · 2012: 41
- FWCI
- 1.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Plant Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Keywords
- Rubisco, photosynthetic carbon assimilation, photorespiration, enzyme catalytic efficiency, oxygen inhibition, carbamoylation, dead-end inhibition, Rubisco activase, enzyme engineering, agricultural productivity
- MeSH terms
- Protein Binding, Protein Conformation, Ribulose-Bisphosphate Carboxylase
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