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Introduction
The RNA lariat debranching enzyme, Dbr1, is a metallophosphoesterase that cleaves 2'-5' phosphodiester bonds within intronic lariats. [3]
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Previous reports have indicated that Dbr1 enzymatic activity is supported by diverse metal ions including Ni2+ , Mn2+ , Mg2+ , Fe2+ , and Zn2+ . [3]
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ICP-AES corroborate this finding, and in vitro debranching assays with fluorescently labeled branched substrates confirm activity. [3]
Function
Figure 1. DPPIV structure
DPPIV, a moonlighting protein, has been implicated in many functions and diseases of the body including glucose metabolism, cardiovascular disease, the stress response, autoimmune diseases (ie HIV/AIDS), inflammation, and tumor biology.
Catalytic Triad
The Catalytic Triad of DPP4 is Ser630, His740, Asp708.
Mechanism
Figure 2. DPPIV Mechanism
The mechanism for the truncation of GLP-1 using DPP4 is a covalent catalysis.
1st Nucleophile is Oxygen on Ser630 and the 2nd Nucleophile is water.
Disease
Relevance
Structural highlights
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