Information on EC 2.7.7.80 - molybdopterin-synthase adenylyltransferase

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

EC NUMBER
COMMENTARY hide
2.7.7.80
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RECOMMENDED NAME
GeneOntology No.
molybdopterin-synthase adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
molybdenum cofactor biosynthesis
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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
additional information
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the human MOCS3 protein contains an N-terminal domain similar to the Escherichia coli MoeB protein. This N-terminal MoeB-like domain is active in catalyzing the adenylyltransferase activity, and C239 of the N-terminal MoeB-like domain of MOCS3 is most likely involved in the sulfur transfer mechanism of the persulfide sulfur to MOCS2A
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 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-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
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
x * 52000, recombinant enzyme, SDS-PAGE
SUBUNITS
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
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
expression of the MOCS3 MoeB-like domain MOCS3-MoeBD in a Esccherichia coli MoeB-deficient strain moeB- (DE3)
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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
ENGINEERING
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
C239A
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the MOCS3 N-terminal domain mutant shows 81% reduced MoeB-like activity compared to wild-type MOCS3, the cysteine 293 residue in the MOCS3-MoeB domain is involved in the sulfur transfer reaction of MOCS3, EC 2.8.1.11
additional information
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the human MOCS3-MoeB domain can be functionally substituted by Escherichia coli MoeB protein
Show AA Sequence (1497 entries)
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