Information on EC 2.10.1.1 - molybdopterin molybdotransferase

for references in articles please use BRENDA:EC2.10.1.1
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

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EC NUMBER
COMMENTARY hide
2.10.1.1
-
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RECOMMENDED NAME
GeneOntology No.
molybdopterin molybdotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP + H2O
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molybdate transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
molybdenum cofactor biosynthesis
Folate biosynthesis
-
-
Metabolic pathways
-
-
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SYSTEMATIC NAME
IUBMB Comments
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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
domain E
SwissProt
Manually annotated by BRENDA team
K-12
SwissProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenylyl-molybdopterin + molybdate + 4 H+
molybdenum cofactor + AMP + H2O
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adenylyl-molybdopterin + molybdate + 4 H+
molybdenum cofactor + AMP + H2O
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
required, less efficient
Ni2+
required, less efficient
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdopterin adenylyltransferase
-
in presence of Mg2+ and ATP
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 2.5
molybdate
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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Show AA Sequence (1652 entries)
Please use the Sequence Search for a specific query.
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LINKS TO OTHER DATABASES (specific for EC-Number 2.10.1.1)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)