Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00142Ribulose bisphosphate carboxylase large chain active site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00142
Ribulose bisphosphate carboxylase (EC 4.1.1.39) (RuBisCO) [1,2] catalyzes the initial step in Calvin's reductive pentose phosphate cycle in plants as well as purple and green bacteria. It consists of a large catalytic unit and a small subunit of undetermined function. In plants, the large subunit is coded by the chloroplastic genome while the small subunit is encoded in the nuclear genome. Molecular activation of RuBisCO by CO2 involves the formation of a carbamate with the epsilon-amino group of a conserved lysine residue. This carbamate is stabilized by a magnesium ion. One of the ligands of the magnesium ion is an aspartic acid residue close to the active site lysine [3]. We developed a pattern which includes both the active site residue and the metal ligand, and which is specific to RuBisCO large chains.
Last update:November 1995 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Miziorko H.M. Lorimer G.H. |
| Title | Ribulose-1,5-bisphosphate carboxylase-oxygenase. | |
| Source | Annu. Rev. Biochem. 52:507-535(1983). | |
| PubMed ID | 6351728 | |
| DOI | 10.1146/annurev.bi.52.070183.002451 |
| 2 | Authors | Akazawa T. Takabe T. Kobayashi H. |
| Source | Trends Biochem. Sci. 9:380-383(1984). |
| 3 | Authors | Andersson I. Knight S. Schneider G. Lindqvist Y. Lundqvist T. Branden C.-I. Lorimer G.H. |
| Source | Nature 337:229-234(1989). |
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