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Literature summary for 4.4.1.11 extracted from

  • Yang, Z.; Sun, X.; Li, S.; Tan, Y.; Wang, X.; Zhang, N.; Yagi, S.; Takakura, T.; Kobayashi, Y.; Takimoto, A.; Yoshioka, T.; Suginaka, A.; Frenkel, E.P.; Hoffman, R.M.
    Circulating half-life of PEGylated recombinant methioninase holoenzyme is highly dose dependent on cofactor pyridoxal-5'-phosphate (2004), Cancer Res., 64, 5775-5778.
    View publication on PubMed

Application

Application Comment Organism
medicine recombinant METase targets the elevated methionine dependence of tumor cells and arrests their growth as well as makes tumors more sensitive to standard chemotherapy agents. The combination of methoxypolyethylene glycol succinimidyl glutarate 5000 recombinant METase treatment with pyridoxal-5'-phosphate infusion suggests an effective clinical strategy for long-term methionine depletion to arrest cancer growth Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-methionine + H2O Mus musculus
-
methanethiol + NH3 + 2-oxobutanoate
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
44
-
methoxypolyethylene glycol succinimidyl glutarate 5000 treated recombinant METase Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-methionine + H2O
-
Mus musculus methanethiol + NH3 + 2-oxobutanoate
-
?

Synonyms

Synonyms Comment Organism
METase
-
Mus musculus
methioninase
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate increases the half-life of methoxypolyethylene glycol succinimidyl glutarate 5000 treated recombinant METase holoenzyme in a dose-dependent manner Mus musculus