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Information on EC 2.10.1.1 - molybdopterin molybdotransferase and Organism(s) Escherichia coli and UniProt Accession P12281

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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.
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This record set is specific for:
Escherichia coli
UNIPROT: P12281
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
Cnx1, MoeA, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molybdate transfer
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
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
-
-
-
?
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
INHIBITOR
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
tungstate
50% inhibition with 75 excess of tungstate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdopterin adenylyltransferase
in presence of Mg2+ and ATP
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K-12
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
molybdenum cofactor biosynthesis
PROTEIN VARIANTS
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team