Function of Molybdenum Insertases

Autor: Kruse, Tobias
Rok vydání: 2022
Předmět:
Zdroj: Molecules : Special Issue State-of-the-Art in Molybdenum Cofactor Research 27 (2022) 17, 5372.-https://doi.org/ 10.3390/molecules27175372--Molecules--Molecules : a journal of synthetic chemistry and natural product chemistry / Molecular Diversity Preservation International--http://www.bibliothek.uni-regensburg.de/ezeit/?2008644--http://www.mdpi.com/journal/molecules--https://www.ncbi.nlm.nih.gov/pmc/journals/3416/--1420-3049--1420-3049
ISSN: 1420-3049
Popis: For most organisms molybdenum is essential for life as it is found in the active site of various vitally important molybdenum dependent enzymes (Mo-enzymes). Here, molybdenum is bound to a pterin derivative called molybdopterin (MPT), thus forming the molybdenum cofactor (Moco). Synthesis of Moco involves the consecutive action of numerous enzymatic reaction steps, whereby molybdenum insertases (Mo-insertases) catalyze the final maturation step, i.e., the metal insertion reaction yielding Moco. This final maturation step is subdivided into two partial reactions, each catalyzed by a distinctive Mo-insertase domain. Initially, MPT is adenylylated by the Mo-insertase G-domain, yielding MPT-AMP which is used as substrate by the E-domain. This domain catalyzes the insertion of molybdate into the MPT dithiolene moiety, leading to the formation of Moco-AMP. Finally, the Moco-AMP phosphoanhydride bond is cleaved by the E-domain to liberate Moco from its synthesizing enzyme. Thus formed, Moco is physiologically active and may be incorporated into the different Mo-enzymes or bind to carrier proteins instead.
Databáze: OpenAIRE
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