Sandbox Reserved 1694

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Function of your protein

Inositol polyphosphate 1-Phosphatase found in the organism Bos Taurus, is an enzyme that removes a phosphate group from a substrate through hydrolysis. Specifically, the phosphomonoester bond is removed from position 1 phosphate of Ins(1,4)P2 or Ins(1,3,4)P3 to yield inositol 4-phosphate or inositol 3,4-bisphosphate. Another function this enzyme does is the regulation of gluconeogenesis and nucleotide metabolism within organisms.

Biological relevance and broader implications

This enzyme is important for this organism, Bos Taurus because it not only does inositol signaling but regulation of gluconeogenesis and nucleotide metabolism which are a couple of important pathways that help the organism function. Not only is INNP1 in cattle but can be found in humans and mice with possible slight variances in the function of the enzyme, though the article just picked one of the many organisms that have this enzyme. However, studying this organism is relevant because it allows us to study lithium-inhibited enzyme structures and functions to better understand them Also, possibly further our knowledge on cellular communication networks and/or cellular pathways (metabolisms) on cellular and molecular levels. This could result in advancements in human medicine and understanding enzymes in the human body on a molecular level on how they work.

Important amino acids

These play an extensive role in interactions between 1-PO4 and 2-PO4 of the substrate to the active site. Also, there are a few different that interact with the inositol ring and help reinforce the binding of the Ins(1,4)P2. ^[3]

Inositol (1,4)-bisphosphate is a that binds in the active site of INPP1D54A. The phosphate (1-PO4) in the substrate serves as a ligand for both the calcium ions. ^[3]

Structural highlights

INPP1D54A contains 13 secondary structural elements of which 10 are alpha helices and 3 are beta-sheets (). Percentage-wise, this enzyme is 77% alpha-helices, 23% beta-sheets. Alpha helix 8 and beta-sheet 2 each contain one catalytic amino acid. Also, helix 6 and 7 and beta-sheet 2 form important interactions with the substrate (have 6 of the 9 amino acids that interact with the substrate).

Other important features

In the structure INPP1D54A, there is a mutation in the amino acid aspartic acid (D)54 and causes it to change to alanine (A)54 (). This mutation does not impact the substrate affinity but does decrease the activity of INPP1. ^[3]

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