{"product_id":"abcam-ab286034","title":"Abcam, ab286034, Recombinant L-methionine gamma-lyase Active protein (mutated F47L + D172E + S308Y)","description":"\u003cp\u003eSize: 200µg\u003cbr\u003e\nRecombinant L-methionine gamma-lyase Active protein (mutated F47L + D172E + S308Y) is a Full Length protein, expressed in Escherichia coli, with \u0026gt;95%, suitable for SDS-PAGE, FuncS, Size Exclusion Chromatography.\u003cbr\u003e\nKey facts\u003cbr\u003e\nPurity:\u0026gt;95% SDS-PAGE,\u003cbr\u003e\nExpression system:Escherichia coli,\u003cbr\u003e\nTags:His tag N-Terminus,\u003cbr\u003e\nApplications:Size Exclusion Chromatography, SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,\u003cbr\u003e\nBiologically active:Yes,\u003cbr\u003e\nBiological activity:Specific activity is ≥ 5 mU\/mg in which one Unit enzyme converts 1 μmole of homocysteine into hydrogen sulfide, per minute at 25 °C and pH 8.1 in the presence of pyridoxal phosphate,\u003cbr\u003e\nAnimal free:Yes,\u003cbr\u003e\nCarrier free:No,\u003cbr\u003e\nStorage buffer:pH: 7.4Constituents: 10.269% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic\u003c\/p\u003e\n\n\u003cp\u003eProperties and Storage Information:\u003cbr\u003e\nShipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C\u003c\/p\u003e\n\n\u003cp\u003eSupplementary Information:\u003cbr\u003e\nThis supplementary information is collated from multiple sources and compiled automatically.\u003cbr\u003e\nL-methionine gamma-lyase also known as methionine gamma-lyase is an enzyme primarily involved in the deamination of L-methionine to produce α-ketobutyrate ammonia and thiol. This enzyme is particularly notable in that it can also degrade S-methyl-L-cysteine and homocysteine therefore playing a role in sulfur amino acid metabolism. L-methionine gamma-lyase has an approximate molecular weight of 172 kDa depending on the organism and is expressed mostly in bacteria such as Pseudomonas putida but not in humans.\u003cbr\u003e\nBiological function summary\u003cbr\u003e\nL-methionine gamma-lyase contributes to the metabolism of sulfur-containing amino acids. It is not typically part of a complex but operates independently to catalyze reactions involving L-methionine transforming it into useful metabolites that organisms like bacteria can utilize effectively. Its activity influences intracellular levels of methionine and sulfur compounds which can affect various biochemical processes including oxidative stress responses and regulation of cellular homeostasis.\u003cbr\u003e\nPathways\u003cbr\u003e\nSulfur amino acid metabolism relies significantly on L-methionine gamma-lyase. This enzyme influences the transsulfuration pathway through which methionine is ultimately converted into cysteine. It interplays with enzymes such as cystathionine gamma-lyase within this pathway. Furthermore its action links methionine metabolism to the broader context of the one-carbon metabolism pathway important for the synthesis of nucleotides and methylation reactions necessary for cell proliferation and gene expression.\u003cbr\u003e\nResearchers have explored L-methionine gamma-lyase as a potential target in cancer therapy due to its ability to affect methionine metabolism important for some tumor growths reliant on high methionine levels. Its activity may also be relevant in bacterial infections where this enzyme's presence in pathogenic bacteria highlights a potential target for antibiotic development. L-methionine gamma-lyase's interaction with human methionine metabolism-related proteins while indirect can significantly impact cellular pathways altered in disease contexts.\u003c\/p\u003e","brand":"Abcam","offers":[{"title":"Default Title","offer_id":46843852128425,"sku":"ab286034","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/ar\/products\/abcam-ab286034","provider":"Iright","version":"1.0","type":"link"}