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Literature summary extracted from

  • Kanaujia, S.P.; Jeyakanthan, J.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Sekar, K.
    Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms (2011), Acta Crystallogr. Sect. F, 67, 2-16.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.75 expressed in Escherichia coli as a His-tagged fusion protein Aquifex aeolicus
4.1.99.22 gene mog, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL Aquifex aeolicus
4.1.99.22 gene mogA, phylogenetic tree, recombinant expression Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.75 crystal structure of AaMogA is determined at 1.7 A resolution (space group P2 resolution), or 1.9 A resolution (space group P1) Aquifex aeolicus
4.1.99.22 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 Aquifex aeolicus
4.1.99.22 purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.64 A resolution, molecular replacement method Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.99.22 additional information
-
 additional information molecular dynamics and docking studies with several small molecules, including substrate and product, binding affinities towards AaMogA, overview Aquifex aeolicus
4.1.99.22 additional information
-
 additional information molecular dynamics and docking studies with several small molecules, including substrate and product, binding affinities towards TtMogA, overview Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.75 Aquifex aeolicus Q5SLF2
-
-
4.1.99.22 Aquifex aeolicus O66472 mog gene, aq_061
-
4.1.99.22 Thermus thermophilus Q5SLF2 gene TTHA0341
-
4.1.99.22 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SLF2 gene TTHA0341
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.75 using Ni-NTA chromatography Aquifex aeolicus
4.1.99.22 recombinant enzyme Thermus thermophilus
4.1.99.22 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 Aquifex aeolicus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.7.75 ATP + H2Dtpp-mP = diphosphate + H2Dtpp-mADP comparative analyses reveal a possible role for the N- and C-terminal residues of MoaB and MogA proteins, respectively, in stabilizing the substrate and/or product molecule in the active site Aquifex aeolicus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.22 additional information binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview Thermus thermophilus ?
-
 ?
4.1.99.22 additional information binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview Aquifex aeolicus ?
-
 ?
4.1.99.22 additional information binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.75 oligomer
-
 Aquifex aeolicus
4.1.99.22 More homology structure comparisons for identification of residues involved in protein oligomerization, overview Thermus thermophilus
4.1.99.22 More homology structure comparisons for identification of residues involved in protein oligomerization, overview Aquifex aeolicus

Synonyms

EC Number Synonyms Comment Organism
2.7.7.75 AaMogA
-
 Aquifex aeolicus
4.1.99.22 Moco-biosynthesis protein
-
 Thermus thermophilus
4.1.99.22 Moco-biosynthesis protein
-
 Aquifex aeolicus
4.1.99.22 MogA
-
 Thermus thermophilus
4.1.99.22 MogA
-
 Aquifex aeolicus
4.1.99.22 molybdenum-cofactor biosynthesis protein
-
 Thermus thermophilus
4.1.99.22 molybdenum-cofactor biosynthesis protein
-
 Aquifex aeolicus