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Information on EC 2.7.7.80 - molybdopterin-synthase adenylyltransferase and Organism(s) Escherichia coli and UniProt Accession P12282

for references in articles please use BRENDA:EC2.7.7.80
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IUBMB Comments
Adenylates the C-terminus of the small subunit of the molybdopterin synthase. This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit. The reaction occurs in prokaryotes and eukaryotes. In the human, the reaction is catalysed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.
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Escherichia coli
UNIPROT: P12282
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mocs3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:molybdopterin-synthase adenylyltransferase
Adenylates the C-terminus of the small subunit of the molybdopterin synthase. This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit. The reaction occurs in prokaryotes and eukaryotes. In the human, the reaction is catalysed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.
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-synthase sulfur-carrier protein]-Gly-Gly
diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
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
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly
diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
MoeB beongs to the MoeB/E1 enzyme superfamily, conserved active site structure, overview. The molybdenum cofactor (Moco) biosynthesis, involving Escherichia coli proteins MoeB and MoaD, is an evolutionarily conserved pathway
malfunction
The Escherichia coli moeB mutant strains contain an inactive, desulfo form of MPT synthase. Substitutions of every cysteine residue in MoeB does not affect activity, except for the mutations in the cysteine residues located in putative Zn-binding motifs, which cause loss of metal binding correlated with loss of activity
metabolism
Escherichia coli proteins MoeB and MoaD are involved in molybdenum cofactor (Moco) biosynthesis
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
x * 52000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 52000, recombinant enzyme, SDS-PAGE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MoeB-MoaD complex in its apo, ATP-bound, and MoaD-adenylate forms, equal volumes of 23 mg/ml MoeB and 10 mg/ml MoaD at 4°C for 1 h, followed by hanging drop vapour diffusion against a reservoir containing 1.7 M Li2SO4, and 100 mM HEPES, pH 7.5, for the ternary complex, crystals of the apo complex are soaked for 24 h in a solution consisting of 1.7 M Li2SO4, 100 mM HEPES, pH 7.5, and 20 mM ATP, X-ray diffraction structure determination and analysis at 1.7-3.5 A resolutions, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C128A
site-directed mutagenesis, completely active mutant
C128Y
site-directed mutagenesis, completely active mutant
C142A
site-directed mutagenesis, the mutant shows activity like the wild-type enzyme
C142A/C187A
site-directed mutagenesis, the mutant shows activity like the wild-type enzyme
C172A
site-directed mutagenesis, the mutant's Zn2+ content is below the limit of detection, the activity is reduced compared to the wild-type enzyme
C175A
site-directed mutagenesis, the mutant's Zn2+ content is below the limit of detection, the activity is reduced compared to the wild-type enzyme
C187A
site-directed mutagenesis, the mutant shows activity like the wild-type enzyme
C231A
site-directed mutagenesis, the mutant shows activity like the wild-type enzyme
C244A
site-directed mutagenesis, the mutant's Zn2+ content is below the limit of detection, the activity is reduced compared to the wild-type enzyme
C247A
site-directed mutagenesis, the mutant's Zn2+ content is below the limit of detection, the activity is reduced compared to the wild-type enzyme
C44A
site-directed mutagenesis, the mutant shows activity like the wild-type enzyme
D130A
site-directed mutagenesis, inactive mutant
D130E
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R14A
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
R14A/R73A
site-directed mutagenesis, inactive mutant
R14K
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
R14K/R73A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R73A
site-directed mutagenesis, the mutant shows slighty reduced activity compared to the wild-type enzyme
R73K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant MoeBs from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene moeB, DNA and amino acid sequence determinations, expression of wild-type MoeB in Escherichia coli strain BL21(DE3) and of MoeB mutants in Escerichia coli strain moeB- (DE3) cells from pMW15eB
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leimkuehler, S.; Wuebbens, M.; Rajagopalan, K.
Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor
J. Biol. Chem.
276
34695-34701
2001
Escherichia coli (P12282)
Manually annotated by BRENDA team
Lake, M.; Wuebbens, M.; Rajagopalan, K.; Schindelin, H.
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
Nature
414
325-329
2001
Escherichia coli (P12282)
Manually annotated by BRENDA team