Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics | Citrobacter freundii | |
0.17 | - |
S-ethyl-L-cysteine | pH and temperature not specified in the publication | Citrobacter freundii | |
1.2 | - |
L-1-amino-3-methylthiopropylphosphinic acid | pH and temperature not specified in the publication | Citrobacter freundii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Citrobacter freundii | Q84AR1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
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 | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
MGL | - |
Citrobacter freundii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Citrobacter freundii |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.6 | - |
L-norleucine | pH and temperature not specified in the publication | Citrobacter freundii |
General Information | Comment | Organism |
---|---|---|
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 |
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 |