Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1. Export

@article{citeulike:2138833, abstract = {Hydroxypyruvate reductase was purified to homogeneity from the facultative methylotroph Methylobacterium extorquens AM1. It has a molecular mass of about 71 kDa, and it consists of two identical subunits with a molecular mass of about 37 kDa. This enzyme uses both NADH (Km = 0.04 mM) and NADPH (Km = 0.06 mM) as cofactors, uses hydroxypyruvate (Km = 0.1 mM) and glyoxylate (Km = 1.5 mM) as the only substrates for the forward reaction, and carries out the reverse reaction with glycerate (Km = 2.6 mM) only. It was not possible to detect the conversion of glycolate to glyoxylate, a proposed role for this enzyme. Kinetics and inhibitory studies of the enzyme from M. extorquens AM1 suggest that hydroxypyruvate reductase is not a site for regulation of the serine cycle at the level of enzyme activity.}, address = {W.M. Keck Laboratories, California Institute of Technology, Pasadena 91125.}, author = {Chistoserdova, L. V. and Lidstrom, M. E.}, citeulike-article-id = {2138833}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/1657886}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=1657886}, issn = {0021-9193}, journal = {J Bacteriol}, keywords = {am1\_enzymes}, month = {November}, number = {22}, pages = {7228--7232}, posted-at = {2007-12-18 00:07:50}, priority = {0}, title = {Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/1657886}, volume = {173}, year = {1991} }

TY - JOUR ID - citeulike:2138833 L3 - citeulike-article-id:2138833 N2 - Hydroxypyruvate reductase was purified to homogeneity from the facultative methylotroph Methylobacterium extorquens AM1. It has a molecular mass of about 71 kDa, and it consists of two identical subunits with a molecular mass of about 37 kDa. This enzyme uses both NADH (Km = 0.04 mM) and NADPH (Km = 0.06 mM) as cofactors, uses hydroxypyruvate (Km = 0.1 mM) and glyoxylate (Km = 1.5 mM) as the only substrates for the forward reaction, and carries out the reverse reaction with glycerate (Km = 2.6 mM) only. It was not possible to detect the conversion of glycolate to glyoxylate, a proposed role for this enzyme. Kinetics and inhibitory studies of the enzyme from M. extorquens AM1 suggest that hydroxypyruvate reductase is not a site for regulation of the serine cycle at the level of enzyme activity. IS - 22 JF - J Bacteriol SN - 0021-9193 AD - W.M. Keck Laboratories, California Institute of Technology, Pasadena 91125. EP - 7232 TI - Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1. VL - 173 SP - 7228 KW - am1_enzymes AU - Chistoserdova, LV AU - Lidstrom, ME PY - 1991/11// UR - http://view.ncbi.nlm.nih.gov/pubmed/1657886 ER -