1WGI

STRUCTURE OF INORGANIC PYROPHOSPHATASE

Summary for 1WGI

• Entry DOI: 10.2210/pdb1wgi/pdb
• Descriptor: INORGANIC PYROPHOSPHATASE, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: pyrophosphate phosphohydrolase, hydrolase, manganese
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P00817
• Total number of polymer chains: 2
• Total formula weight: 64670.50

Authors

Heikinheimo, P.,Goldman, A. (deposition date: 1996-10-24, release date: 1997-11-19, Last modification date: 2024-02-14)

Primary citation

Heikinheimo, P.,Lehtonen, J.,Baykov, A.,Lahti, R.,Cooperman, B.S.,Goldman, A.
The structural basis for pyrophosphatase catalysis.
Structure, 4:1491-1508, 1996

PubMed Abstract: Soluble inorganic pyrophosphatase (PPase), an essential enzyme central to phosphorus metabolism, catalyzes the hydrolysis of the phosphoanhydride bond in inorganic pyrophosphate. Catalysis requires divalent metal ions which affect the apparent pKas of the essential general acid and base on the enzyme, and the pKa of the substrate. Three to five metal ions are required for maximal activity, depending on pH and enzyme source. A detailed understanding of catalysis would aid both in understanding the nature of biological mechanisms of phosphoryl transfer, and in understanding the role of divalent cations. Without a high-resolution complex structure such a model has previously been unobtainable.

PubMed: 8994974
DOI: 10.1016/S0969-2126(96)00155-4

Experimental method

X-RAY DIFFRACTION (2.2 Å)