mutase

Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyzes the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. GPM1 Protein, S. cerevisiae, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 29.5 kDa and the accession number is P00950.

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B. Required for normal osteoclastogenesis.

Bisphosphoglycerate Mutase (BPGM) is a member of the Phosphoglycerate Mutase family and BPG-Dependent PGAM subfamily. BPGM is a multifunctional enzyme. BPGM catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. It also has phosphoglycerate phosphomutase activity. BPGM plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Deficiency of BPGM increases the affinity of cells for oxygen and result in hemolytic anemia.

Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle. MMUT Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 84.8 kDa and the accession number is P22033.

Mutc Protein, Mouse, Recombinant (His) is expressed in E. coli.

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Superoxide dismutase [Fe] Protein, Anabaena sp., Recombinant (His & KSI) is expressed in E. coli expression system with N-6xHis-KSI tag. The predicted molecular weight is 16.4 kDa and the accession number is P83157.

UBASH3B contains a ubiquitin associated domain at the N-terminus, an SH3 domain, and a C-terminal domain with similarities to the catalytic motif of phosphoglycerate mutase. UBASH3B was found to inhibit endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor. UBASH3B interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. It promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. UBASH3B exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP7. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.

6-phosphofructo-2-kinase fructose-2,6-bisphosphatase 1 is an enzyme that in humans is encoded by the PFKFB1 gene. The enzyme forms a homodimer that catalyzes both the synthesis and degradation of fructose-2,6-biphosphate using independent catalytic domains. It belongs to the phosphoglycerate mutase family. Fructose-2,6-biphosphate is an activator of the glycolysis pathway and an inhibitor of the gluconeogenesis pathway. Consequently, regulating fructose-2,6-biphosphate levels through the activity of this enzyme is thought to regulate glucose homeostasis.

Lactoylglutathione lyase, also known as Methylglyoxalase, Aldoketomutase, Glyoxalase I, Ketone-aldehyde mutase, S-D-lactoylglutathione methylglyoxal lyase and GLO1, is a member of the glyoxalase I family. GLO1 Glyoxalase I is a ubiquitous cellular defense enzyme involved in the detoxification of methylglyoxal, a cytotoxic byproduct of glycolysis. Accumulative evidence suggests an important role of GLO1 expression in protection against methylglyoxal-dependent protein adduction and cellular damage associated with diabetes, cancer, and chronological aging. GLO1 Glyoxalase I has been implicated in anxiety-like behavior in mice and in multiple psychiatric diseases in humans. GLO1 Glyoxalase I catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. GLO1 Glyoxalase I exists in three separable isoforms which originate from two alleles in the genome. These correspond to two homodimers and one heterodimer composed of two subunits showing different electrophoretic properties. GLO1 upregulation may play a functional role in glycolytic adaptations of cancer cells.