Mechanistic divergence between (4S,7R)-germacra-(1(10)E,5E)-dien-11-ol synthases from Dictyostelium purpureum and Streptomyces coelicolor

2021 ◽  
Author(s):  
Houchao Xu ◽  
Jan Rinkel ◽  
Xinlu Chen ◽  
Tobias G. Köllner ◽  
Feng Chen ◽  
...  
Keyword(s):  
Streptomyces Coelicolor ◽  
Enzyme Mechanism ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Dictyostelium Purpureum

The enzyme mechanism of germacradienol synthase DpTPS9 from Dictyostelium purpureum has been studied by labelling experiments and site-directed mutagenesis, and is different to the mechanism of geosmin synthase SCO6073 from Streptomyces coelicolor.

A structural perspective on the enzymes that convert dTDP-d-glucose into dTDP-l-rhamnose

2003 ◽  
Vol 31 (3) ◽  
pp. 532-536 ◽  
Author(s):  
C. Dong ◽  
K. Beis ◽  
M.-F. Giraud ◽  
W. Blankenfeldt ◽  
S. Allard ◽  
...  
Keyword(s):  
Pathogenic Bacteria ◽  
Structural Data ◽  
Enzyme Mechanism ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Human Pathogens ◽  
Biochemical Pathways ◽  
Short Chain Dehydrogenase ◽  
Mycobacteria Tuberculosis ◽  
Shed Light

Bacteria have a rich collection of biochemical pathways for the synthesis of complex metabolites. These conversions often involve chemical reactions that are hard to reproduce in the laboratory. An area of considerable interest is in the manipulation and synthesis of carbohydrates. In contrast with amino acids, carbohydrates are densely functionalized (each carbon atom is attached to at least one heteroatom) and this holds out the prospect of discovering novel enzyme mechanisms. The results from the study of the biosynthetic dTDP-l-rhamnose pathway are discussed. dTDP-l-rhamnose is a key intermediate in many pathogenic bacteria, as it is the donor for l-rhamnose, which is found in the cell wall of important human pathogens, such as Mycobacteria tuberculosis and Salmonella typhimurium. All four enzymes have been structurally characterized; in particular, the acquisition of structural data on substrate complexes was extremely useful. The structural data have guided site-directed-mutagenesis studies that have been used to test mechanistic hypotheses. The results shed light on three classes of enzyme mechanism: nucleotide condensation, short-chain dehydrogenase activity and epimerization.

Isoishwarane synthase from Streptomyces lincolnensis

2021 ◽  
Author(s):  
Houchao Xu ◽  
Jan Rinkel ◽  
Jeroen S. Dickschat
Keyword(s):  
Natural Product ◽  
Enzyme Mechanism ◽  
Site Directed Mutagenesis ◽  
Terpene Synthase ◽  
Directed Mutagenesis ◽  
Isotopic Labelling ◽  
Streptomyces Lincolnensis ◽  
Isotopic Labelling Experiments

The product of a terpene synthase from Streptomyces lincolnensis has been identified as the new natural product isoishwarane. The enzyme mechanism was studied by isotopic labelling experiments and site-directed mutagenesis.

The site-directed mutagenesis and prokaryotic expression of midkine gene in Cynoglossus semilaevis

2013 ◽  
Vol 37 (3) ◽  
pp. 330
Author(s):  
Yanan WANG ◽  
Xudong LIU ◽  
Linlin MU ◽  
Zhipeng LIU ◽  
Chunmei LI ◽  
...  
Keyword(s):  
Prokaryotic Expression ◽  
Cynoglossus Semilaevis ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis
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