Information on EC 2.7.7.75 - molybdopterin adenylyltransferase

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

EC NUMBER
COMMENTARY hide
2.7.7.75
-
RECOMMENDED NAME
GeneOntology No.
molybdopterin adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Folate biosynthesis
-
-
Metabolic pathways
-
-
molybdenum cofactor biosynthesis
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+.
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
-
efficient inhibition at 1-10 mM diphosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
-
activating by 5 units in the standard reaction set-up
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
ATP
Arabidopsis thaliana
-
10 mM MgCl2, pH 7.2, temperature not specified in the publication
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain J99 / ATCC 700824)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-nitrilotriacetic acid matrix
using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cnx1 G-domain in pQE60
expressed in Escherichia coli as a His-tagged fusion protein
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
Show AA Sequence (516 entries)
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