Information on EC 2.7.7.75 - molybdopterin adenylyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
2.7.7.75
-
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RECOMMENDED NAME
GeneOntology No.
molybdopterin adenylyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group 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
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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
domain G; commentary
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
ATP + molybdopterin
diphosphate + adenylyl-molybdopterin
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
ATP + molybdopterin
diphosphate + adenylyl-molybdopterin
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
required
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
-
efficient inhibition at 1-10 mM diphosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
-
activating by 5 units in the standard reaction set-up
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.062
ATP
-
10 mM MgCl2, pH 7.2, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
ATP
-
10 mM MgCl2, pH 7.2, temperature not specified in the publication
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
Q9ZL45
Helicobacter pylori (strain J99 / ATCC 700824);
Q8U3T3
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-nitrilotriacetic acid matrix
using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cnx1 G-domain in pQE60
expressed in Escherichia coli as a His-tagged fusion protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D486A
-
inactive
D515N
-
in Cnx1 G-domain, accumulation of molybdopterin
N597L
-
in Cnx1 G-domain, strong decrease in molybdopterin binding
R547E
-
decreased activity
S476A
-
inactive
S573A
-
inactive in absence of pyrophosphatase, decreased actitivity in presence of pyrophosphatase
S583A
-
increased activity
T542A
-
decreased activity
T542D
-
inactive
T542S
-
decreased activity
V557G
-
in Cnx1 G-domain, strong decrease in molybdopterin binding
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Show AA Sequence (702 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.7.75)
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)