Recombinant L-methionine .gamma.-lyase

Drug – bio-affecting and body treating compositions – Enzyme or coenzyme containing – Transferases

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435232, 536 232, A61K 3851, C12N 988, C07H 2104

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active

058611541

ABSTRACT:
A recombinant protein capable of constituting a recombinant L-methionine .gamma.-lyase or a variant thereof, a recombinant oligomeric enzyme, preferably tetrameric enzyme, consisting of the recombinant protein, a DNA molecule encoding the same, an expression vector containing the DNA molecule, a host cell harboring the expression vector, a method of preparing the recombinant L-methionine .gamma.-lyase, and anti-tumor agent comprising the recombinant L-methionine .gamma.-lyase or a variant thereof are provided.

REFERENCES:
Nakayama et al.(Jul. 1984) Purification of Bacterial L-Methionine gamma-Lyase Analytical Biochemistry 138: 421-424.
Erickson et al. (Jul. 1990) Sequence of cDNA for rat cystathionine gamma-lyase and comparison of deduced amino acid sequence with related Escherichia coli enzymes, Biochemical Journal 269: 335-340.
Rudinger, J. (Jun. 1976) Characteristics of the amino acids as components of a peptide hormone sequence, In Peptide Hormones, Ed. J. A. Parsons, University Park Press, pp. 1-7.
Ngo et al. (Jan. 1994) Computational complexity, protein structure prediction, and the ILevinthal paradox. In: The Protein Folding Problem and Tertiary Structure Prediction. Eds. Merz et al. Birkhauser et al. Boston, Ma. pp. 491-495.
Thornton et al. (Sep. 1995) Protein Engineering: Editorial Overview. Current Opinion in Biotechnology 6(4): 367-369.
Wallace (Apr. 1993) Understanding cytochrome c function: engineering protein structure by semisynthesis. The FASEB Journal 7: 505-515.
JB vol. 117, No. 5 May 1995, "The Journal of Biochemistry".
Nakayama et al, Biochemistry, 27, pp. 1587-1591 (1988).
Lishko et al, Protein Expression and Purification, 4, pp. 529-533 (1993).
Nippon Nogeikagaku Kaisha, 68, p. 106 (Mar. 3, 1994).

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