8ron
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/FAD1_HUMAN FAD1_HUMAN] Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.<ref>PMID:16643857</ref> <ref>PMID:27259049</ref> | [https://www.uniprot.org/uniprot/FAD1_HUMAN FAD1_HUMAN] Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.<ref>PMID:16643857</ref> <ref>PMID:27259049</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human flavin adenine dinucleotide synthase (hFADS) is a bifunctional, multi-domain enzyme that exhibits both flavin mononucleotide adenylyltransferase and pyrophosphatase activities. Here we report the crystal structure of full-length hFADS2 and its C-terminal PAPS domain in complex with flavin adenine dinucleotide (FAD), and dissect the structural determinants underlying the contribution of each individual domain, within isoforms 1 and 2, to each of the two enzymatic activities. Structural and functional characterization performed on complete or truncated constructs confirmed that the C-terminal domain tightly binds FAD and catalyzes its synthesis, while the combination of the N-terminal molybdopterin-binding and KH domains is the minimal essential substructure required for the hydrolysis of FAD and other ADP-containing dinucleotides. hFADS2 associates in a stable C2-symmetric dimer, in which the packing of the KH domain of one protomer against the N-terminal domain of the other creates the adenosine-specific active site responsible for the hydrolytic activity. | ||
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| + | Structural insights into the bifunctional enzyme human FAD synthase.,Leo G, Leone P, Ataie Kachoie E, Tolomeo M, Galluccio M, Indiveri C, Barile M, Capaldi S Structure. 2024 Jul 11;32(7):953-965.e5. doi: 10.1016/j.str.2024.04.006. Epub , 2024 Apr 29. PMID:38688286<ref>PMID:38688286</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8ron" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of human FAD synthase, isoform 2
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