Moco Carrier and Binding Proteins

Autor: Tobias, Kruse
Jazyk: angličtina
Rok vydání: 2022
Předmět:
Zdroj: Molecules : Special Issue State-of-the-Art in Molybdenum Cofactor Research 27 (2022) 19, 6571.-https://doi.org/10.3390/molecules27196571--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
Popis: The molybdenum cofactor (Moco) is the active site prosthetic group found in numerous vitally important enzymes (Mo-enzymes), which predominantly catalyze 2 electron transfer reactions. Moco is synthesized by an evolutionary old and highly conserved multi-step pathway, whereby the metal insertion reaction is the ultimate reaction step here. Moco and its intermediates are highly sensitive towards oxidative damage and considering this, they are believed to be permanently protein bound during synthesis and also after Moco maturation. In plants, a cellular Moco transfer and storage system was identified, which comprises proteins that are capable of Moco binding and release but do not possess a Moco-dependent enzymatic activity. The first protein described that exhibited these properties was the Moco carrier protein (MCP) from the green alga Chlamydomonas reinhardtii. However, MCPs and similar proteins have meanwhile been described in various plant species. This review will summarize the current knowledge of the cellular Moco distribution system.
Databáze: OpenAIRE