Image:PEPC reaction mechanism.png
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Summary
Catalytic mechanism of PEPC based on maize C4-PEPC and E. coli PEPC crystal structures and the three-step reaction model. The hydrophobic pocket is shown as yellow circles and the residues show maize numbering. Adapted from Izui K, Matsumura H, Furumoto T, Kai Y. Phosphoenolpyruvate carboxylase: a new era of structural biology. Annu Rev Plant Biol. 2004;55:69-84. PMID:15725057 doi:10.1146/annurev.arplant.55.031903.141619
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Date/Time | User | Dimensions | File size | Comment | |
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(current) | 00:26, 30 June 2023 | Karsten Theis (Talk | contribs) | 1024×502 | 48 KB | From https://commons.wikimedia.org/wiki/File:PEP_Carboxylase_Mechanism.png, Tims2015, CC BY-SA 3.0 <https://creativecommons.org/licenses/by-sa/3.0>, via Wikimedia Commons |
23:41, 25 June 2023 | Lucas Xavier da Cunha (Talk | contribs) | 611×400 | 160 KB | Catalytic mechanism of PEPC based on maize C4-PEPC and E. coli PEPC crystal structures and the three-step reaction model. The hydrophobic pocket is shown as yellow circles and the residues show maize numbering. Adapted from Izui K, Matsumura H, Furumoto T | |
22:42, 25 June 2023 | Lucas Xavier da Cunha (Talk | contribs) | 1078×706 | 397 KB | Catalytic mechanism of PEPC based on maize C4-PEPC and E. coli PEPC crystal structures and the three-step reaction model. The hydrophobic pocket is shown as yellow circles and the residues show maize numbering. Adapted from Izui K, Matsumura H, Furumoto |
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