EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.6.1.17 | purified recombinant MoaC2s in apo form, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution | Mycobacterium tuberculosis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.6.1.17 | 17500 | - |
2 * 17500, MoaC2 functional form | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.6.1.17 | GTP | Mycobacterium tuberculosis | - |
cyclic pyranopterin phosphate + diphosphate | - |
? | |
4.6.1.17 | GTP | Mycobacterium tuberculosis H37Rv | - |
cyclic pyranopterin phosphate + diphosphate | - |
? | |
4.6.1.17 | additional information | Mycobacterium tuberculosis | the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate) | ? | - |
? | |
4.6.1.17 | additional information | Mycobacterium tuberculosis H37Rv | the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate) | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.6.1.17 | Mycobacterium tuberculosis | P9WJR7 | MoaC2; gene Rv0864 | - |
4.6.1.17 | Mycobacterium tuberculosis H37Rv | P9WJR7 | MoaC2; gene Rv0864 | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.6.1.17 | GTP = cyclic pyranopterin phosphate + diphosphate | mechanisms proposed for the first step of the Moco biosynthesis pathway, overview | Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.6.1.17 | GTP | - |
Mycobacterium tuberculosis | cyclic pyranopterin phosphate + diphosphate | - |
? | |
4.6.1.17 | GTP | - |
Mycobacterium tuberculosis H37Rv | cyclic pyranopterin phosphate + diphosphate | - |
? | |
4.6.1.17 | additional information | the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate) | Mycobacterium tuberculosis | ? | - |
? | |
4.6.1.17 | additional information | molecular docking studies with probable ligands suggests that pteridinebenzomonophosphate is the most likely ligand. Molybdenum cofactor biosynthesis protein A1, MoaA1, and MoaC2 interact with each other in a complex and do not act independently of each other, homology modeling of MoaA1 complexed with MoaC2 and protein-protein interaction analysis, detailed docking study, overview | Mycobacterium tuberculosis | ? | - |
? | |
4.6.1.17 | additional information | the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate) | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
4.6.1.17 | additional information | molecular docking studies with probable ligands suggests that pteridinebenzomonophosphate is the most likely ligand. Molybdenum cofactor biosynthesis protein A1, MoaA1, and MoaC2 interact with each other in a complex and do not act independently of each other, homology modeling of MoaA1 complexed with MoaC2 and protein-protein interaction analysis, detailed docking study, overview | Mycobacterium tuberculosis H37Rv | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.6.1.17 | dimer | 2 * 17500, MoaC2 functional form | Mycobacterium tuberculosis |
4.6.1.17 | hexamer | MoaC2 mainly forms hexamers, which are not functional | Mycobacterium tuberculosis |
4.6.1.17 | More | tertiary and quaternary structures of MoaC2, detailed overview | Mycobacterium tuberculosis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.6.1.17 | MoaC2 | - |
Mycobacterium tuberculosis |
4.6.1.17 | Moco-biosynthesis protein | - |
Mycobacterium tuberculosis |
4.6.1.17 | molybdenum cofactor biosynthesis protein C | - |
Mycobacterium tuberculosis |