Literature summary for 4.4.1.11 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.

Crystallization (Commentary)

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

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

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 [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Citrobacter freundii	Q84AR1	-	-

Substrates and Products (Substrate)

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

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

Synonyms	Comment	Organism
MGL	-	Citrobacter freundii

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Citrobacter freundii

Ki Value [mM]

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

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