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EC Tree
IUBMB Comments Catalyses the activation of molybdopterin for molybdenum insertion. In eukaryotes, this reaction is catalysed by the C-terminal domain of a fusion protein that also includes molybdopterin molybdotransferase (EC 2.10.1.1). The reaction requires a divalent cation such as Mg2+ or Mn2+.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
AaMogA,
Cnx1 ,
MogA ,
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Cnx1
C-terminal G-domain, gene name
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ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
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ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
comparative analyses reveal a possible role for the N- and C-terminal residues of MoaB and MogA proteins, respectively, in stabilizing the substrate and/or product molecule in the active site
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nucleotidyl group transfer
nucleotidyl group transfer
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nucleotidyl group transfer
-
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ATP:molybdopterin adenylyltransferase
Catalyses the activation of molybdopterin for molybdenum insertion. In eukaryotes, this reaction is catalysed by the C-terminal domain of a fusion protein that also includes molybdopterin molybdotransferase (EC 2.10.1.1). The reaction requires a divalent cation such as Mg2+ or Mn2+.
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ATP + molybdopterin
diphosphate + adenylyl-molybdopterin
ATP + molybdopterin
diphosphate + adenylyl-molybdopterin
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-
-
?
ATP + molybdopterin
diphosphate + adenylyl-molybdopterin
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-
-
?
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ATP + molybdopterin
diphosphate + adenylyl-molybdopterin
ATP + molybdopterin
diphosphate + adenylyl-molybdopterin
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-
-
?
ATP + molybdopterin
diphosphate + adenylyl-molybdopterin
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-
-
?
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Mg2+
required
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diphosphate
efficient inhibition at 1-10 mM diphosphate
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diphosphate
activating by 5 units in the standard reaction set-up
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0.062
ATP
10 mM MgCl2, pH 7.2, temperature not specified in the publication
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0.0012
ATP
10 mM MgCl2, pH 7.2, temperature not specified in the publication
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UniProt
brenda
domain G; commentary
SwissProt
brenda
K-12
SwissProt
brenda
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metabolism
molybdenum cofactor biosynthesis
metabolism
molybdenum cofactor biosynthesis
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crystal structure of AaMogA is determined at 1.7 A resolution (space group P2 resolution), or 1.9 A resolution (space group P1)
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D515N
in Cnx1 G-domain, accumulation of molybdopterin
N597L
in Cnx1 G-domain, strong decrease in molybdopterin binding
S573A
inactive in absence of pyrophosphatase, decreased actitivity in presence of pyrophosphatase
V557G
in Cnx1 G-domain, strong decrease in molybdopterin binding
D515H
inactive
D515H
in Cnx1 G-domain, accumulation of molybdopterin
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Ni-nitrilotriacetic acid matrix
using Ni-NTA chromatography
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expressed in Escherichia coli as a His-tagged fusion protein
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Llamas, A.; Mendel, R.R.; Schwarz, G.
Synthesis of adenylated molybdopterin: an essential step for molybdenum insertion
J. Biol. Chem.
279
55241-55246
2004
Arabidopsis thaliana (Q39054)
brenda
Nichols, J.D.; Rajagopalan, K.V.
In vitro molybdenum ligation to molybdopterin using purified components
J. Biol. Chem.
280
7817-7822
2005
Escherichia coli (P0AF03)
brenda
Kuper, J.; Palmer, T.; Mendel, R.R.; Schwarz, G.
Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin binding, molybdenum insertion, and molybdenum cofactor stabilization
Proc. Natl. Acad. Sci. USA
97
6475-6480
2000
Arabidopsis thaliana (Q39054)
brenda
Kanaujia, S.P.; Jeyakanthan, J.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Sekar, K.
Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms
Acta Crystallogr. Sect. F
67
2-16
2011
Aquifex aeolicus (Q5SLF2), Aquifex aeolicus
brenda
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History
Enzyme Nomenclature
2.7.7.75 molybdopterin adenylyltransferase
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