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EC Tree
IUBMB 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.
The enzyme appears in viruses and cellular organisms
Synonyms
Cnx1 ,
MoeA ,
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Cnx1
N-terminal E-domain, gene name
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adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP + H2O
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-
-
-
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molybdate transfer
-
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adenylyl-molybdopterin:molybdate molybdate transferase (AMP-forming)
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.
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adenylyl-molybdopterin + molybdate + 4 H+
molybdenum cofactor + AMP + H2O
adenylyl-molybdopterin + molybdate + 4 H+
molybdenum cofactor + AMP + H2O
-
-
-
?
adenylyl-molybdopterin + molybdate + 4 H+
molybdenum cofactor + AMP + H2O
-
-
-
?
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adenylyl-molybdopterin + molybdate + 4 H+
molybdenum cofactor + AMP + H2O
adenylyl-molybdopterin + molybdate + 4 H+
molybdenum cofactor + AMP + H2O
-
-
-
?
adenylyl-molybdopterin + molybdate + 4 H+
molybdenum cofactor + AMP + H2O
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-
-
?
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Mn2+
required, less efficient
Ni2+
required, less efficient
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glutathione
50% inhibition at 0.4 mM
L-cysteine
50% inhibition at 0.01 mM
molybdopterin adenylyltransferase
in absence of Mg2+ and ATP
-
Na2S
50% inhibition at 1.3 mM
sulfate
less efficient inhibition than tungstate
tungstate
20fold excess to molybdate
tungstate
50% inhibition with 75 excess of tungstate
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molybdopterin adenylyltransferase
in presence of Mg2+ and ATP
-
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0.25
molybdate
in presence of Mg2+, pH 7.2, temperature not specified in the publication
2.5
molybdate
in presence of Zn2+, pH 7.2, temperature not specified in the publication
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domain E
SwissProt
brenda
K-12
SwissProt
brenda
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metabolism
molybdenum cofactor biosynthesis
metabolism
molybdenum cofactor biosynthesis
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D142N
high activity in vitro
D228A
wild type activity in vitro
D228N
wild type activity in vitro
D259A
high activity in vitro
D59A
high activity in vitro
D59N
high activity in vitro
delPhe53-Arg139
inactive in vivo, low activity in vitro
E188A
wild type activity in vitro
E188Q
wild type activity in vitro
K275Q
decreased activity in vitro
K279Q
low activity in vitro
R137Q
decreased activity in vitro
R350A
low activity in vitro
S271A
decreased activity in vitro
S371W
low activity in vitro
T100A
decreased activity in vitro
T100W
decreased activity in vitro
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Nichols, J.D.; Xiang, S.; Schindelin, H.; Rajagopalan, K.V.
Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft
Biochemistry
46
78-86
2007
Escherichia coli (P12281)
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 (P12281)
brenda
Llamas, A.; Otte, T.; Multhaup, G.; Mendel, R.R.; Schwarz, G.
The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly
J. Biol. Chem.
281
18343-18350
2006
Arabidopsis thaliana (Q39054)
brenda
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Enzyme Nomenclature
2.10.1.1 molybdopterin molybdotransferase
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