AI Article Synopsis
- - Corynebacterium glutamicum is important for making amino acids, nucleotides, and vitamins, and it relies on the shikimate pathway enzymes DAHP synthase (CgDS) and chorismate mutase (CgCM) for producing aromatic compounds.
- - The study found that CgCM needs to form a complex with CgDS to work properly, and both enzymes are regulated by aromatic amino acids; amino acids like phenylalanine and tyrosine inhibit CgCM, while tryptophan activates it.
- - Detailed crystal structures of CgCM, CgDS, and their complex revealed how these interactions occur on a molecular level, showing that DAHP synthase plays a crucial role
Article Abstract
Corynebacterium glutamicum is widely used for the industrial production of amino acids, nucleotides, and vitamins. The shikimate pathway enzymes DAHP synthase (CgDS, Cg2391) and chorismate mutase (CgCM, Cgl0853) play a key role in the biosynthesis of aromatic compounds. Here we show that CgCM requires the formation of a complex with CgDS to achieve full activity, and that both CgCM and CgDS are feedback regulated by aromatic amino acids binding to CgDS. Kinetic analysis showed that Phe and Tyr inhibit CgCM activity by inter-enzyme allostery, whereas binding of Trp to CgDS strongly activates CgCM. Mechanistic insights were gained from crystal structures of the CgCM homodimer, tetrameric CgDS, and the heterooctameric CgCM-CgDS complex, refined to 1.1, 2.5, and 2.2 Å resolution, respectively. Structural details from the allosteric binding sites reveal that DAHP synthase is recruited as the dominant regulatory platform to control the shikimate pathway, similar to the corresponding enzyme complex from Mycobacterium tuberculosis.
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| http://dx.doi.org/10.1021/acs.biochem.7b01018 | DOI Listing |
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