GLXR Protein, Mouse (His-SUMO)

GLXR is a multifunctional enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase activities. It promotes the conversion of hydroxypyruvic acid into D-glyceric acid, glyoxylic acid into glycolic acid, and oxidation of D-glyceric acid into hydroxypyruvic acid. GLXR Protein, Mouse (His-SUMO) is the recombinant mouse-derived GLXR protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag. The total length of GLXR Protein, Mouse (His-SUMO) is 328 a.a., with molecular weight of ~51.3 kDa.

The GLXR protein, characterized by its multifunctional enzymatic activities, acts as a hydroxy-pyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase. Its versatile enzymatic functions involve the reduction of hydroxypyruvate to D-glycerate and glyoxylate to glycolate, while also oxidizing D-glycerate to hydroxypyruvate. This dynamic enzymatic profile suggests a pivotal role for GLXR in the interconversion of key metabolites within cellular pathways. The ability of GLXR to catalyze these reactions reflects its importance in metabolic processes where hydroxy-pyruvate, glyoxylate, and D-glycerate are involved, emphasizing its significance in maintaining metabolic homeostasis (

Mouse

E. coli

N-6*His;N-SUMO

Q91Z53 (M1-L328)

76238  [NCBI]

MKPARLMKVFVTGPLPAEGRAALAQAADCEVEQWNSDDPIPRKDLEQGVVGAHGLLCRLSDRVDKKLLDAAGANLRVISTLSVGVDHLALDEIKKRGIRVGYTPGVLTDATAELAVSLLLTTCRRLPEAIEEVKNGGWSSWSPLWMCGYGLSQSTVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPDTMGLCSKDFFQKMKNTAIFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSLLAANNLLAGLRGEAMPSELKL

Approximately 51.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.