8IXI

Crystal structure of macrolide phosphotransferase from Klebsiella pneumoniae

Summary for 8IXI

• Entry DOI: 10.2210/pdb8ixi/pdb
• Descriptor: Macrolide 2'-phosphotransferase (2 entities in total)
• Functional Keywords: macrolide 2'-phosphotransferase, transferase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 67699.54

Authors

Zhang, Z.L.,Gao, C. (deposition date: 2023-04-01, release date: 2024-01-31, Last modification date: 2024-10-23)

Primary citation

Zhang, Z.,Chu, R.,Wei, W.,Song, W.,Ye, C.,Chen, X.,Wu, J.,Liu, L.,Gao, C.
Systems engineering of Escherichia coli for high-level glutarate production from glucose.
Nat Commun, 15:1032-1032, 2024

PubMed Abstract: Glutarate is a key monomer in polyester and polyamide production. The low efficiency of the current biosynthetic pathways hampers its production by microbial cell factories. Herein, through metabolic simulation, a lysine-overproducing E. coli strain Lys5 is engineered, achieving titer, yield, and productivity of 195.9 g/L, 0.67 g/g glucose, and 5.4 g/L·h, respectively. Subsequently, the pathway involving aromatic aldehyde synthase, monoamine oxidase, and aldehyde dehydrogenase (AMA pathway) is introduced into E. coli Lys5 to produce glutarate from glucose. To enhance the pathway's efficiency, rational mutagenesis on the aldehyde dehydrogenase is performed, resulting in the development of variant Mu5 with a 50-fold increase in catalytic efficiency. Finally, a glutarate tolerance gene cbpA is identified and genomically overexpressed to enhance glutarate productivity. With enzyme expression optimization, the glutarate titer, yield, and productivity of E. coli AMA06 reach 88.4 g/L, 0.42 g/g glucose, and 1.8 g/L·h, respectively. These findings hold implications for improving glutarate biosynthesis efficiency in microbial cell factories.

PubMed: 38310110
DOI: 10.1038/s41467-024-45448-z

Experimental method

X-RAY DIFFRACTION (2.28 Å)