Molecular cloning and characterization of a phosphoglycerate mutase gene from Clonorchis sinensis.
Phosphoglycerate mutase (PGM) is a widely distributed glycolytic enzyme. Two known distinct classes of PGM enzymes were identified, a cofactor-dependent one (dPGM) and a cofactor-independent one (iPGM). A complementary DNA (cDNA) encoding a PGM was cloned from a Clonorchis sinensis cDNA library by large-scale sequencing. This new cDNA contains 955 bp with a putative open reading frame of 256 amino acids, which has a high homology with dPGMs from a number of species. The putative peptide was produced in E. coli and was purified to electrophoretic homogeneity. Enzymatic assays showed that the product of this gene could catalyze the conversion of 3-phosphoglycerate to 2-phosphoglycerate when the cofactor was present and the enzyme activities could be inhibited by vanadate.
Song
Linxia
L
College of Life Science, Shandong University of Technology, Zibo 255049, People's Republic of China.
Xu
Zhenbiao
Z
Yu
Xinbing
X
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003004:Clonorchis sinensis / Q000201:enzymology* / Q000235:genetics; D019295:Computational Biology; D015723:Gene Library; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D010736:Phosphoglycerate Mutase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D017422:Sequence Analysis, DNA
D015801:Helminth Proteins; D010736:Phosphoglycerate Mutase