Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: kinetic and x-ray study

Kinetic and ultraviolet-visible spectral techniques were utilized to investigate the interaction of Escherichia coli cystathionine beta lyase (CBL) and aminoethoxyvinylglycine (AVG). The results indicated that AVG can act as a slow-binding inhibitor of CBL. X-ray crystallography revealed the spatial structure of the CBLAVG complex as compatible with a ketimine as the reaction product. The structure suggested a binding mode for rhizobitoxine.