Structural highlights
Function
D9IEF7_BPT4 MARC1_HUMAN As a component of an N-hydroxylated prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively.[1]
Publication Abstract from PubMed
A study recently published in Hepatology Communications provided insights into a variant of MTARC1 protein, which conveys protection against liver disease. Here, we report a crystal structure of the variant protein at near-atomic resolution and compare it to the structure of the wildtype protein.
Letter to the editor: The clinically relevant MTARC1 p.Ala165Thr variant impacts neither the fold nor active site architecture of the human mARC1 protein.,Struwe MA, Clement B, Scheidig A Hepatol Commun. 2022 May 13. doi: 10.1002/hep4.1984. PMID:35560545[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gruenewald S, Wahl B, Bittner F, Hungeling H, Kanzow S, Kotthaus J, Schwering U, Mendel RR, Clement B. The fourth molybdenum containing enzyme mARC: cloning and involvement in the activation of N-hydroxylated prodrugs. J Med Chem. 2008 Dec 25;51(24):8173-7. doi: 10.1021/jm8010417. PMID:19053771 doi:http://dx.doi.org/10.1021/jm8010417
- ↑ Struwe MA, Clement B, Scheidig A. Letter to the editor: The clinically relevant MTARC1 p.Ala165Thr variant impacts neither the fold nor active site architecture of the human mARC1 protein. Hepatol Commun. 2022 May 13. doi: 10.1002/hep4.1984. PMID:35560545 doi:http://dx.doi.org/10.1002/hep4.1984
