Information on EC 4.1.99.18 - cyclic pyranopterin phosphate synthase

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

EC NUMBER
COMMENTARY hide
4.1.99.18
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RECOMMENDED NAME
GeneOntology No.
cyclic pyranopterin phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP = cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Folate biosynthesis
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Metabolic pathways
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molybdenum cofactor biosynthesis
SYSTEMATIC NAME
IUBMB Comments
GTP 8,9-lyase (cyclic pyranopterin monophosphate-forming)
The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). The enzyme MoaA from bacteria and the human enzyme MOCS1A each contain two oxygen-sensitive FeS clusters. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. In bacteria, the reaction is catalysed by MoaA and requires the action of MoaC. The latter protein is equivalent to the C-terminal domain of the eukaryotic enzyme MOCS1A which does not need further protein components to perform the reaction.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mog gene, aq_061
UniProt
Manually annotated by BRENDA team
Arthrobacter nicotinovorans
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SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
show the reaction diagram
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
additional information
?
-
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
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
reaction of MoaC
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-
?
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
show the reaction diagram
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reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC
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?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
iron-sulfur centre
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MoaC protein
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00006 - 0.00079
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
additional information
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Staphylococcus aureus (strain NCTC 8325)
Staphylococcus aureus (strain NCTC 8325)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
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monomer, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da), gel filtration
82000
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homodimer, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da), gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
monomer
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1 * 42000, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da)
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, mixing of 0.001 ml of 24 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 0.2 M NaCl, with 0.001 ml of reservoir solution containing 40% v/v PEG 600, 100 mM CHES buffer, pH 9.5, or 0.2 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, 25% w/v PEG 3350, 1 week, two different crystal forms, X-ray diffraction structure determination and analysis at 1.7-1.9 A resolution, molecular replacement method
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.003 ml of 10.5 mg/ml protein solution with 0.0015 ml reservoir solution containing 0.025 M potassium sodium tartrate tetrahydrate, pH 8.0, and equilibration against 1 ml reservoir solution, 15 days, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement calculations
purified recombinant MoaC2s in apo form, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
crystal structure of wild-type MoaA, MoaA-R17A/R266A/R268A and MoaA in complex with 5'-GTP2.35 A resolution
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crystals are grown under anaerobic conditions, hanging drop vapor diffusion technique, crystals belong to space group P2(1)2(1)2(1) with cell dimensions of a = 48.1, b = 102.4, and c = 191.2 A and contain two molecules per asymmetric unit, structures of MoaA in the apo-state (2.8 A) and in complex with S-adenosyl-L-methionine (2.2 A)
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sitting-drop method, hanging-drop vapour-diffusion method, at room temperature
GTP-bound crystal structure
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purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.64 A resolution, molecular replacement method
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified under anaerobic conditions
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recombinant enzyme
recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by two different times of gel filtration and anion exchange chromatography, followed by gel filtration and hydroxyapatite chromatography, and a last step of gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography and gel filtration
recombinant MOCS1B from Escherichia coli strain BL21(DE3) by streptomycin sulfate and ammonium sulfate precipitation steps, nickel affinity chromatography, gell filtration, and ultrafiltration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His-tagged proteins in Escherichia coli
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expression in Escherichia coli
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gene mog, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
gene mogA, phylogenetic tree, recombinant expression
gene Rv0864, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
MOCS1B overexpression in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is downregulated by 3times in the nutrient starvation model for Mycobacterium tuberculosis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C24S/C28S/C31S
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the mutant does not contain the catalytic S-adenosyl-L-methionine-binding cluster I
N124A/N165A
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mutation reduces binding of 5'-GTP
R17A
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complete loss of activity
R17A/R266A/R268A
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complete loss of activity
R192A
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80% loss of activity
R266A
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complete loss of activity
R268A
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complete loss of activity
R71A
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80% loss of activity
S126A
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mutant enzyme with low activity
T73A
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mutant enzyme with low activity
Y30A
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mutant enzyme with low activity
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