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UniProt functional annotation for P13254 | ||
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| UniProt code: P13254. |
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| Organism: | |
Pseudomonas putida (Arthrobacter siderocapsulatus). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas. |
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| Function: | |
Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia (PubMed:8586629, PubMed:6742420). Is involved in L-methionine catabolism (PubMed:9190812). In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol compounds, alpha,gamma-elimination and gamma-replacement reactions of L- homocysteine and its S-substituted derivatives, O-substituted-L- homoserines and DL-selenomethionine, and, to a lesser extent, alpha,beta-elimination and beta-replacement reactions of L-cysteine, S- methyl-L-cysteine, and O-acetyl-L-serine (PubMed:6742420, PubMed:22785484). Also catalyzes deamination and gamma-addition reactions of L-vinylglycine (PubMed:6742420). Thus, the enzyme is able to cleave C-S, C-Se, and C-O bonds of sulfur, selenium, and oxygen amino acids, respectively (PubMed:6742420, PubMed:22785484). {ECO:0000269|PubMed:22785484, ECO:0000269|PubMed:6742420, ECO:0000269|PubMed:8586629, ECO:0000305|PubMed:9190812}. |
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| Catalytic activity: | |
Reaction=H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+); Xref=Rhea:RHEA:23800, ChEBI:CHEBI:15377, ChEBI:CHEBI:16007, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; EC=4.4.1.11; Evidence={ECO:0000269|PubMed:22785484, ECO:0000269|PubMed:6742420}; |
| Catalytic activity: | |
Reaction=H2O + L-homocysteine = 2-oxobutanoate + H(+) + hydrogen sulfide + NH4(+); Xref=Rhea:RHEA:14501, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919, ChEBI:CHEBI:58199; EC=4.4.1.2; Evidence={ECO:0000269|PubMed:22785484, ECO:0000269|PubMed:6742420}; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:17289792, ECO:0000269|PubMed:22785484, ECO:0000269|PubMed:6742420}; |
| Activity regulation: | |
Irreversibly inactivated by DL-propargylglycine. {ECO:0000269|PubMed:22785484}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=1.0 mM for L-methionine {ECO:0000269|PubMed:6742420}; KM=0.5 mM for L-methionine {ECO:0000269|PubMed:22785484}; KM=1.1 mM for DL-homocysteine {ECO:0000269|PubMed:22785484}; KM=0.2 mM for L-cysteine {ECO:0000269|PubMed:22785484}; KM=0.7 mM for S-methyl-L-cysteine {ECO:0000269|PubMed:22785484}; KM=7.2 mM for O-succinyl-L-homoserine {ECO:0000269|PubMed:22785484}; Note=kcat is 33.4 sec(-1) for the alpha,gamma-elimination of L- methionine. kcat is 71.0 sec(-1) for the alpha,gamma-elimination of DL-homocysteine. kcat is 2.13 sec(-1) for the alpha,beta-elimination of L-cysteine. kcat is 1.58 sec(-1) for the alpha,beta-elimination of S-methyl-L-cysteine. kcat is 2.56 sec(-1) for the alpha,gamma- elimination of O-succinyl-L-homoserine. {ECO:0000269|PubMed:22785484}; |
| Subunit: | |
Homotetramer; dimer of active dimers. {ECO:0000269|PubMed:17289792, ECO:0000269|PubMed:6742420}. |
| Induction: | |
Is under the control of the positive transcriptional regulator MdeR. Forms part of an operon with mdeB. {ECO:0000269|PubMed:9190812}. |
| Biotechnology: | |
The recombinant MGL protein cloned form P.putida has been found to have antitumor efficacy in vitro and in vivo. PEGylated MGL is being developed as a cancer drug. {ECO:0000303|PubMed:25439528}. |
| Similarity: | |
Belongs to the trans-sulfuration enzymes family. L- methionine gamma-lyase subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.