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Literature summary for 4.1.99.22 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
Search for more literature for 4.1.99.22

Cloned(Commentary)

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate Staphylococcus aureus reaction of MoaC cyclic pyranopterin phosphate + diphosphate
-
 ?
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
-
 ?
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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Staphylococcus aureus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate reaction of MoaC Staphylococcus aureus cyclic pyranopterin phosphate + diphosphate
-
 ?
(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 ?
(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 ?
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
-
 ?
GTP reaction of MoaA Staphylococcus aureus (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate NMR spectroscopy product analysis ?
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 ?
-
 ?
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

Synonyms Comment Organism
MoaA
-
 Staphylococcus aureus
MoaC
-
 Staphylococcus aureus
MOCS1B
-
 Homo sapiens

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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