Function
Cystathionine gamma synthase (CGS) catalyzes the formation of cystathionine and succinate from cysteine and succinyl homoserine in microorganisms and plants. This reaction is part of Met biosynthesis pathway[1].
Relevance
CGS deletion mutants in bacteria caused lack of growth which was reversed by addition of Met[2]. CGS is a target of antimicrobial agent and herbicides.
Structural highlights
The 3D structure of tobacco CGS complex with an inhibitor shows the interaction of the inhibitor in the substrate binding pocket of CGS dimer. The carboxylate moiety of the inhibitor makes hydrogen bond to Arg and its phosphonate group binds to phosphate recognition group formed by residues from both monomers[3].
- ↑ Flavin M, Slaughter C. Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine. Biochim Biophys Acta. 1967 Mar 15;132(2):400-5. doi:, 10.1016/0005-2744(67)90158-1. PMID:5340123 doi:https://dx.doi.org/10.1016/0005-2744(67)90158-1
- ↑ Fu J, Wu J, Jiang J, Wang Z, Ma Z. Cystathionine gamma-synthase is essential for methionine biosynthesis in Fusarium graminearum. Fungal Biol. 2013 Jan;117(1):13-21. doi: 10.1016/j.funbio.2012.11.001. Epub 2012 , Dec 1. PMID:23332829 doi:https://dx.doi.org/10.1016/j.funbio.2012.11.001
- ↑ Steegborn C, Laber B, Messerschmidt A, Huber R, Clausen T. Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor. J Mol Biol. 2001 Aug 24;311(4):789-801. PMID:11518531 doi:10.1006/jmbi.2001.4880