Methylamine utilisation protein
From Proteopedia
(Difference between revisions)
(New page: <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> == Function == '''Methylamine utilisation protein'''. (MauG) is a 2 c type heme prot...) |
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== Function == | == Function == | ||
| - | '''Methylamine utilisation protein'''. (MauG) is a 2 c type heme protein (in which the heme is covalently bound to the protein) which catalyses the post translational modification of tryptophan cryptophilquinone biosynthesis within methylamine dehydrogenase. The catalysis process is a remote one involving hole hopping mechanism of electron transfer in which Top residues are reversibly oxidized<ref>PMID:24144526</ref>. | + | '''Methylamine utilisation protein'''. (MauG) is a 2 c type heme protein (in which the heme is covalently bound to the protein) which catalyses the post translational modification of tryptophan cryptophilquinone biosynthesis within methylamine dehydrogenase (MADH). The catalysis process is a remote one involving hole hopping mechanism of electron transfer in which Top residues are reversibly oxidized<ref>PMID:24144526</ref>. MauG catalyses the 6-electron oxidation of MADH using hydrogen peroxide or oxygen. |
== Disease == | == Disease == | ||
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== References == | == References == | ||
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Revision as of 09:34, 9 August 2022
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References
- ↑ Shin S, Davidson VL. MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis. Arch Biochem Biophys. 2014 Feb 15;544:112-8. doi: 10.1016/j.abb.2013.10.004. Epub, 2013 Oct 19. PMID:24144526 doi:http://dx.doi.org/10.1016/j.abb.2013.10.004
