1eav

Structural highlights

Function

CNX1_ARATH Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.^{[1] [2] [3] [4]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Gephyrin

References

1. ↑ Llamas A, Mendel RR, Schwarz G. Synthesis of adenylated molybdopterin: an essential step for molybdenum insertion. J Biol Chem. 2004 Dec 31;279(53):55241-6. Epub 2004 Oct 25. PMID:15504727 doi:http://dx.doi.org/10.1074/jbc.M409862200
2. ↑ Llamas A, Otte T, Multhaup G, Mendel RR, Schwarz G. The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly. J Biol Chem. 2006 Jul 7;281(27):18343-50. Epub 2006 Apr 24. PMID:16636046 doi:http://dx.doi.org/10.1074/jbc.M601415200
3. ↑ Kuper J, Winking J, Hecht HJ, Mendel RR, Schwarz G. The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G. Arch Biochem Biophys. 2003 Mar 1;411(1):36-46. PMID:12590921
4. ↑ Kuper J, Llamas A, Hecht HJ, Mendel RR, Schwarz G. Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism. Nature. 2004 Aug 12;430(7001):803-6. PMID:15306815 doi:10.1038/nature02681