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Literature summary extracted from

  • Hover, B.M.; Loksztejn, A.; Ribeiro, A.A.; Yokoyama, K.
    Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis (2013), J. Am. Chem. Soc., 135, 7019-7032.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.22 MOCS1B overexpression in Escherichia coli strain BL21(DE3) Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.99.22 0.00006
-
 (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate pH 7.6, 25°C, MOCS1B Homo sapiens
4.1.99.22 0.00079
-
 (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate pH 7.6, 25°C, MoaC Staphylococcus aureus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.99.22 Fe2+ MoaA harbors two [4Fe-4S]2+,1+ clusters, the N-terminal is used for reductive cleavage of S-adenosyl-L-methionine, the C-terminal [4Fe-4S] cluster binds various purine nucleoside 5'-triphosphates including GTP Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.22 (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate Staphylococcus aureus reaction of MoaC cyclic pyranopterin phosphate + diphosphate
-
 ?
4.1.99.22 GTP Staphylococcus aureus reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
-
 ?
4.1.99.22 additional information Staphylococcus aureus MoaA catalyzes a unique radical C-C bond formation reaction via a 5'-deoxyadenosyl radical intermediate and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.22 Homo sapiens
-
-
-
4.1.99.22 Staphylococcus aureus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.22 recombinant MOCS1B from Escherichia coli strain BL21(DE3) by streptomycin sulfate and ammonium sulfate precipitation steps, nickel affinity chromatography, gell filtration, and ultrafiltration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.22 (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate reaction of MoaC Staphylococcus aureus cyclic pyranopterin phosphate + diphosphate
-
 ?
4.1.99.22 (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate reaction of MoaC, which is responsible for the formation of the cyclic phosphate Staphylococcus aureus cyclic pyranopterin phosphate + diphosphate NMR spectroscopy product analysis ?
4.1.99.22 (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate reaction of MOCS1B, responsible for the formation of the cyclic phosphate Homo sapiens cyclic pyranopterin phosphate + diphosphate NMR spectroscopy product analysis ?
4.1.99.22 GTP reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC Staphylococcus aureus (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
-
 ?
4.1.99.22 GTP reaction of MoaA Staphylococcus aureus (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate NMR spectroscopy product analysis ?
4.1.99.22 additional information MoaA catalyzes a unique radical C-C bond formation reaction via a 5'-deoxyadenosyl radical intermediate and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring Staphylococcus aureus ?
-
 ?
4.1.99.22 additional information MoaA/C coupled assay. MoaA catalyzes a unique radical C-C bond formation reaction and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring Staphylococcus aureus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.22 MoaA
-
 Staphylococcus aureus
4.1.99.22 MoaC
-
 Staphylococcus aureus
4.1.99.22 MOCS1B
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.22 25
-
 assay at, MoaA and MoaC Staphylococcus aureus
4.1.99.22 25
-
 assay at, MOCS1B Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.22 7.6
-
 assay at, MoaA and MoaC Staphylococcus aureus
4.1.99.22 7.6
-
 assay at, MOCS1B Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.22 S-adenosyl-L-methionine MoaA as a radical S-adenosyl-L-methionine enzyme Staphylococcus aureus