ArticleACS catalysis2024
Elucidation of the stereochemical mechanism of cystathionine γ-lyase reveals how substrate specificity constrains catalysis.
Article in ACS catalysis, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Carboxyl-directed, general α-site-selective deuteration of carboxylic acids by PdNature communications · 2026Article
- Family-Specialized Transformer for L-cystathionine gamma-lyase Engineering and Its Structural Interpretation.Computational and structural biotechnology journal · 2026Article
- Molecular Basis for Cγ-N Bond Formation by PLP-Dependent Enzyme LolC.Biochemistry · 2024Article
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4 authors.
Funding
Abstract
Pyridoxal phosphate (PLP)-dependent enzymes play essential roles in metabolism and have found applications for organic synthesis and as enzyme therapeutics. The vinylglycine ketimine (VGK) subfamily hosts a growing set of enzymes that play diverse roles in primary and secondary metabolism. However, the molecular determinates of substrate specificity and the complex acid-base chemistry that enables VGK catalysis remain enigmatic. We use a recently discovered amino acid γ-lyase as a model system to probe catalysis in this enzyme family. We discovered that two stereochemically distinct proton transfer pathways occur. Combined kinetic and spectroscopic analysis revealed that progression through the catalytic cycle is correlated with the presence of an H-bond donor after Cγ of an amino acid substrate, suggesting substrate binding is kinetically coupled to a conformational change. High-resolution X-ray crystallography shows that cystathionine-γ-lyases generate an
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