摘要： 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR), also known as isoprenoid synthesis H (IspH) or lysis-tolerant B (LytB), catalyzes the last step of the methylerythritol phosphate pathway to synthesize isopentenyl diphosphate and dimethylallyl diphosphate. The structure and reaction mechanism of IspH have been actively investigated in Escherichia coli but little is known in plants. Compared with the bacterial IspH, cyanobacterial and plant HDRs all contain an extra N-terminal conserved domain (NCD) that is essential for their function. Tyr72 in the NCD and several plant-specific residues around the central active site are critical for Arabidopsis HDR function. These results suggest that the structure and reaction mechanism of HDR/IspH may be different between plants and bacteria. The E. coli IspH is an iron-sulfur protein that is sensitive to oxygen. It is possible that the cyanobacterial HDR may independently evolve from the common ancestor of prokaryotes to obtain the NCD, which may protect the enzyme from high concentration of oxygen during photosynthesis. 其他題名： Plant Signal Behav 出版者： United States: Taylor & Francis 出版日期： 2015-01-01 出處： Plant signaling & behavior, 2015-01, Vol.10 (2), p.e988072 資源來源： Taylor & Francis Journals Auto-Holdings Collection 版權： 2015 Taylor & Francis Group, LLC 2015 版權： 2015 Taylor & Francis Group, LLC 2015 Taylor & Francis Group, LLC 識別號： ISSN: 1559-2316 識別號： ISSN: 1559-2324 識別號： EISSN: 1559-2324 識別號： DOI: 10.4161/15592324.2014.988072 識別號： PMID: 25723575
