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Numerous malignant cell lines, including those responsible for some gastric and colon cancers, have an elevated dependence on methionine relative to ordinary cells. Treatment of these cancers with enzymes that reduce free methionine has been shown to slow or arrest tumor growth. When deprived of methionine, cells can synthesize it from the similar amino acid homocysteine. We have recently solved the structure of the enzyme L-homocysteine α, γhydrolyase (obtained from Trichomonas vaginalis ) which transaminates homocysteine. The structure of homocysteinase is similar to that of other α, γhydrolases such as L-methionine α, γ-hydrolyase. In conjunction with methioninase, homocysteinase is expected to enhance cancer treatment, especially if its activity and half-life can be increased by mutation. Further investigation of the interactions involved, such as the binding of pyridoxal 5' phosphate (PLP), will elucidate the mechanisms of this type of enzyme.

Crystal structure of full length HPr kinase/phosphatase fromMycoplasma pneumoniae