ExplorEnz: EC 2.10.1.1

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2.10.1.1

Accepted name:

molybdopterin molybdotransferase

Reaction:

adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP + H₂O

For diagram of MoCo biosynthesis, click here

Glossary:

molybdopterin = H2Dtpp-mP = [(5aR,8R,9aR)-2-amino-4-oxo-6,7-bis(sulfanyl)-4,5,5a,8,9a,10-hexahydro-1H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogen phosphate
molybdate = tetraoxidomolybdate(2^-) = MoO₄^2-
molybdenum cofactor = MoCo = MoO2(OH)Dtpp-mP = {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-bis(sulfanyl-κS)-1,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2^-) phosphate}(dioxo)molybdate

Other name(s):

MoeA; Cnx1 (ambiguous)

Systematic name:

adenylyl-molybdopterin:molybdate molybdate transferase (AMP-forming)

Comments:

Catalyses the insertion of molybdenum into the ene-dithiol group of molybdopterin. In eukaryotes this reaction is catalysed by the N-terminal domain of a fusion protein whose C-terminal domain catalyses EC 2.7.7.75, molybdopterin adenylyltransferase. Requires divalent cations such as Mg²⁺ or Zn²⁺ for activity.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Nichols, J.D. and Rajagopalan, K.V. In vitro molybdenum ligation to molybdopterin using purified components. J. Biol. Chem. 280 (2005) 7817–7822. [DOI] [PMID: 15632135]
2.	Nichols, J.D., Xiang, S., Schindelin, H. and Rajagopalan, K.V. Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft. Biochemistry 46 (2007) 78–86. [DOI] [PMID: 17198377]
3.	Llamas, A., Otte, T., Multhaup, G., Mendel, R.R. and Schwarz, G. The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly. J. Biol. Chem. 281 (2006) 18343–18350. [DOI] [PMID: 16636046]

[EC 2.10.1.1 created 2011]