Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase.
Jedrzejas
M J
MJ
Department of Microbiology, University of Alabama at Birmingham, 933 19th Street South, CHSB-19 room 545, Birmingham, AL 35-294-2041, USA. jedrzejas@uab.edu
D000135:Acid Phosphatase / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D000595:Amino Acid Sequence; D001665:Binding Sites; D019143:Evolution, Molecular; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D025481:Phosphofructokinase-2; D010736:Phosphoglycerate Mutase / Q000737:chemistry* / Q000235:genetics* / Q000502:physiology*; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D017386:Sequence Homology, Amino Acid
D025481:Phosphofructokinase-2; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases; D010736:Phosphoglycerate Mutase