The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). In bacteria and plants the reaction is catalysed by MoaC and Cnx3, respectively. In mammals the reaction is catalysed by the MOCS1B domain of the bifuctional MOCS1 protein, which also catalyses EC 4.1.99.22, GTP 3',8-cyclase.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). In bacteria and plants the reaction is catalysed by MoaC and Cnx3, respectively. In mammals the reaction is catalysed by the MOCS1B domain of the bifuctional MOCS1 protein, which also catalyses EC 4.1.99.22, GTP 3',8-cyclase.
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)
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)
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
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
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)
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)
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
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
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)
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)
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)
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)
compound is converted to an analogue of the MoaC reaction intermediate and causes mechanism-based inhibition. the reaction product harbors an acid-labile triaminopyrimidinone base without an established pyranopterin structure and forms a tight complex with MoaC likely through a covalent linkage
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Overexpression, purification, crystallization and preliminary X-ray analysis of putative molybdenum cofactor biosynthesis protein C (MoaC2) from Mycobacterium tuberculosis H37Rv.
expression of genes moaABC of Escherichia coli results in accumulation of a pteridine named compound Z, an intermediate in biosynthesis of molydopterin. The carbon atoms of a pentose or pentulose are diverted to the ring atoms C6 and C7 and to the side chain atoms C2', C3' and C4' of compound Z. Carbon atom C1' of compound Z is derived from carbon atom C8 of a guanine derivative
in molybdopterin biosynthesis, a guanosine derivative serves as the initial biosynthetic precursor. Both the ribose and ring carbon atoms of the guanosine are utilized in this synthesis. The C-8 carbon of the guanosine precursor is retained and incorporated as the first carbon of the molybdopterin side chain
the physiological function of MoaA is the conversion of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate (GTP 3?,8-cyclase), and that of MoaC is to catalyze the rearrangement of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate into cyclic pyranopterin
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the first two enzymes of the molybdopterin biosynthesis pathway are encoded by the MOCS1 locus in humans. Isoform MOCS1A and isoform MOCS1B form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate. They are encoded by an apparently bicistronic MOCS1AMOCS1B transcript which bypasses the normal termination nonsense codon of MOCS1A resulting in fusion of the MOCS1A and MOCS1B open reading frames. The bicistronic form of MOCS1 mRNA is likely to only produce MOCS1A protein and suggests that MOCS1B is translated only as a fusion with MOCS1A
Overexpression, purification, crystallization and preliminary X-ray analysis of putative molybdenum cofactor biosynthesis protein C (MoaC2) from Mycobacterium tuberculosis H37Rv