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A versatile bacterial enzyme:l-methionine γ-lyase

Authors
Journal
Enzyme and Microbial Technology
0141-0229
Publisher
Elsevier
Publication Date
Volume
7
Issue
11
Identifiers
DOI: 10.1016/0141-0229(85)90094-8
Keywords
  • Amino Acids
  • L-Methionine γ-Lyase
  • Pseudomonas Putida
  • Aeromonas Sp.
Disciplines
  • Biology

Abstract

Abstract The properties and application of l-methionine γ-lyase [methioninase, l-methionine methanethiol-lyase (deaminating), EC 4.4.1.11], a pyridoxal 5′-phosphate enzyme, purified from Pseudomonas putida and Aeromonas sp. are presented. The enzyme has multicatalytic functions: it catalyses α,γ-elimination and γ-replacement reactions of l-methionine and its analogues (e.g. ethionine, homocysteine, O-acetylhomoserine and selenomethionine), α,β-elimination and β-replacement reactions of l-cysteine and its analogues (e.g. S-methylcysteine, O-acetylserine and Se-methylselenocysteine), deamination and γ-addition of vinylglycine, and deuterium labelling at the α and β positions of l-methionine and other straight-chain l-amino acids. These reactions are applicable to the synthesis of various optically active sulphur and selenium amino acids, preparation of deuterium or tritium labelled l-amino acids, and determination of sulphur amino acids. In addition, the enzyme shows potent anti-neoplastic activity .

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