show all | hide all No of entries

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

for references in articles please use BRENDA:EC2.10.1.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Escherichia coli
UNIPROT: P12281
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Escherichia coli
Synonyms
Cnx1, MoeA, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MoeA
291766
gene name
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molybdate transfer
-
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
Select items on the left to see more content.