Comparison of the binuclear metalloenzymes diphosphoglycerate-independent phosphoglycerate mutase and alkaline phosphatase: their mechanism of catalysis via a phosphoserine intermediate.
Jedrzejas
M J
MJ
Department of Microbiology, University of Alabama at Birmingham, 933 19th Street South, CHSB-19 Room 545, Birmingham, Alabama 35294, USA. jedrzejas@uab.edu
Setlow
P
P
D000469:Alkaline Phosphatase / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D020404:Glycerophospholipids / Q000378:metabolism*; D008969:Molecular Sequence Data; D010736:Phosphoglycerate Mutase / Q000737:chemistry / Q000378:metabolism*; D010768:Phosphoserine / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D020404:Glycerophospholipids; D010768:Phosphoserine; D000469:Alkaline Phosphatase; D010736:Phosphoglycerate Mutase