9MSA
Alpha-ketoisovalerate decarboxylase (Kivd) from Synechocystis sp. PCC 6803 with substitution S286T
Summary for 9MSA
Entry DOI | 10.2210/pdb9msa/pdb |
Descriptor | Alpha-ketoisovalerate decarboxylase, THIAMINE DIPHOSPHATE, 1,2-ETHANEDIOL, ... (5 entities in total) |
Functional Keywords | synechocystis, isobutanol production, 3-methyl-1-butanol, alpha-ketoisovalerate decarboxylase, kivd, lyase |
Biological source | Lactococcus lactis subsp. lactis |
Total number of polymer chains | 4 |
Total formula weight | 245144.03 |
Authors | |
Primary citation | Xie, H.,Begum, A.,Gunn, L.H.,Lindblad, P. Directed evolution of alpha-ketoisovalerate decarboxylase for improved isobutanol and 3-methyl-1-butanol production in cyanobacteria. Biotechnol Biofuels Bioprod, 18:84-84, 2025 Cited by PubMed Abstract: Cyanobacteria are promising platforms for metabolic engineering to convert carbon dioxide into valuable fuels and chemicals, addressing both energy demands and global climate change. Among various fuels and chemicals, isobutanol (IB) and 3-methyl-1-butanol (3M1B) have gained increasing attention due to their superior physical properties, such as high energy density, low water solubility, and low hygroscopicity. Heterologously expressing α-ketoisovalerate decarboxylase (Kivd) in the unicellular cyanobacterium Synechocystis sp. PCC 6803 (Synechocystis) enables microbial production of IB and 3M1B through the 2-keto acid pathway, with Kivd identified as a key bottleneck limiting production efficiency. PubMed: 40745552DOI: 10.1186/s13068-025-02687-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
Download full validation report
