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Literature summary extracted from

  • Revtovich, S.V.; Morozova, E.A.; Khurs, E.N.; Zakomirdina, L.N.; Nikulin, A.D.; Demidkina, T.V.; Khomutov, R.M.
    Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates (2011), Biochemistry (Moscow), 76, 564-570.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.4.1.11 enzyme in complex with gamma-(L-1-amino-3-methylthiopropylphosphinic acid), beta-(S-ethyl-L-cysteine), and L-norleucine, soaking of holoenzyme crystals in a cryoprotective solution containing 35% PEG monomethyl ether 2000, 50 mM Tris-HCl, pH 8.5, 0.2 mM pyridoxal 5'-phosphate, 25 mM DTT, with addition of the respective ligand, 6.8 mM of beta-(S-ethyl-L-cysteine), 40 mM L-norleucine, or 48 mM gamma-(L-1-amino-3-methylthiopropylphosphinic acid), during different time intervals of 5-120 min, 1-2 weeks, X-ray diffraction structure determination and anaysis at 1.45-1.84 A resolution, molecular replacement Citrobacter freundii

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.4.1.11 L-norleucine Arg374 and Ser339 are involved in the binding of carboxyl groups of the inhibitor, the hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acid Citrobacter freundii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.4.1.11 additional information
-
 additional information steady-state kinetics Citrobacter freundii
4.4.1.11 0.17
-
 S-ethyl-L-cysteine pH and temperature not specified in the publication Citrobacter freundii
4.4.1.11 1.2
-
 L-1-amino-3-methylthiopropylphosphinic acid pH and temperature not specified in the publication Citrobacter freundii

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.11 Citrobacter freundii Q84AR1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.11 L-1-amino-3-methylthiopropylphosphinic acid + H2O Arg374 and Ser339 are involved in the binding of carboxyl groups of the substrate, the hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acid Citrobacter freundii methanethiol + NH3 + propanoylphosphinic acid
-
 ?
4.4.1.11 S-ethyl-L-cysteine + H2O Arg374 and Ser339 are involved in the binding of carboxyl groups of the substrate, the hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acid. Formation of external aldimine, conformational changes in the active center enable the Tyr58 hydroxyl group to occupy a position favorable for protonation of the leaving group Citrobacter freundii ethanethiol + NH3 + pyruvate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.4.1.11 tetramer dimer of dimers, each dimer contains two active centers formed by amino acid residues of both subunits of the dimer. The protein monomer consists of three domains: N-terminal, central PLP-binding, and C-terminal Citrobacter freundii

Synonyms

EC Number Synonyms Comment Organism
4.4.1.11 MGL
-
 Citrobacter freundii

Cofactor

EC Number Cofactor Comment Organism Structure
4.4.1.11 pyridoxal 5'-phosphate
-
 Citrobacter freundii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.4.1.11 0.6
-
 L-norleucine pH and temperature not specified in the publication Citrobacter freundii

General Information

EC Number General Information Comment Organism
4.4.1.11 evolution the enzyme belongs to the subclass of cystathionine beta-lyase with type I folding of the polypeptide chain of pyridoxal 5'-phosphate-dependent enzymes Citrobacter freundii
4.4.1.11 physiological function the pyridoxal5'-phosphate-dependent enzyme catalyzes the gamma-elimination and gamma-replacement of L-methionine and its derivatives and the reactions of beta-elimination and beta-replacement of L-cysteine and S-substituted L-cysteines. The enzyme also catalyzes the reactions of gamma-elimination and gamma-replacement of the phosphinic analogue of methionine, Met-PH. Met-PH has a high antibacterial activity, is an effective fungi cide under field conditions, and inhibits the growth of tumor cells due to transformation into a metabolically stable phosphonic analog of S-adenosylmethionine Citrobacter freundii