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Phosphatases binding site comparison

The crystal structure of recombinant bovine inositol polyphosphate 1-phosphatase (1-ptase) was determined in the presence of Mg + at 2.3-A resolution (York et al., 1994). The fold of 1-ptase is similar to that of two other metaI-dependent/Li+-sensitive phosphatases, inositol monophosphate phosphatase and fructose 1,6-biphosphatase. Comparison of the active-site pockets of these proteins will likely provide insight into substrate binding, the mechanisms of metal-dependent catalysis, and Li+ inhibition. [Pg.272]


See other pages where Phosphatases binding site comparison is mentioned: [Pg.117]    [Pg.399]    [Pg.1287]    [Pg.484]    [Pg.229]    [Pg.173]    [Pg.174]    [Pg.124]    [Pg.229]    [Pg.55]    [Pg.321]    [Pg.572]    [Pg.1888]   
See also in sourсe #XX -- [ Pg.114 ]




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