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Information on EC 4.6.1.17 - cyclic pyranopterin monophosphate synthase
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4.6.1.17 cyclic pyranopterin monophosphate synthaseIUBMB Comments
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
Reaction Schemes
Synonyms
moac2, molybdenum cofactor biosynthesis protein c, st0472, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cnx3
-
-
-
-
EC 4.1.99.18
-
-
formerly, part transferred
-
MoaC
MoaC2
Moco-biosynthesis protein
MOCS1B
molybdenum cofactor biosynthesis protein C
ST0472
MoaC
-
-
-
-
MoaC
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
MoaC
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
MoaC
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
MoaC
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
MOCS1B
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
-
-
-
-
GTP = cyclic pyranopterin phosphate + diphosphate
mechanisms proposed for the first step of the Moco biosynthesis pathway, overview
GTP = cyclic pyranopterin phosphate + diphosphate
mechanisms proposed for the first step of the Moco biosynthesis pathway, overview
-
-
GTP = cyclic pyranopterin phosphate + diphosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate lyase (cyclic pyranopterin phosphate-forming)
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
(8S)-3',8-cyclo-7,8-dihydroguanosine-P[CH2]PP
cyclic pyranopterin phosphate + diphosphate
-
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
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)
-
-
?
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)
-
-
?
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
-
-
?
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
-
-
?
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)
-
-
?
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)
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
?
additional information
?
-
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
?
additional information
?
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
?
additional information
?
-
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
?
additional information
?
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
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)
-
-
?
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)
-
-
?
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)
-
-
?
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)
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-P-CH2-PP
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
additional information
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
additional information
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
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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.
Tuberculosis
Structural Insights into Putative Molybdenum Cofactor Biosynthesis Protein C (MoaC2) from Mycobacterium tuberculosis H37Rv.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00021
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
His-tagged wild-type, pH not specified in the publication, temperature not specified in the publication
0.00025
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.001
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
mutant K51A, pH not specified in the publication, temperature not specified in the publication
0.0016
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
mutant H77A, pH not specified in the publication, temperature not specified in the publication
0.0024
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
mutant E112A, pH not specified in the publication, temperature not specified in the publication
0.0043
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
mutant E114A, pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
mutant K51A, pH not specified in the publication, temperature not specified in the publication
0.00004
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
mutant E114A, pH not specified in the publication, temperature not specified in the publication
0.00004
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
mutant H77A, pH not specified in the publication, temperature not specified in the publication
0.00005
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
mutant E112A, pH not specified in the publication, temperature not specified in the publication
0.0088
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0093
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
His-tagged wild-type, pH not specified in the publication, temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
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
physiological function
-
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
physiological function
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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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
additional information
hexamer
MoaC2 mainly forms hexamers, which are not functional
additional information
tertiary and quaternary structures of MoaC2, detailed overview
additional information
-
tertiary and quaternary structures of MoaC2, detailed overview
additional information
-
tertiary and quaternary structures of MoaC2, detailed overview
-
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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
purified recombinant MoaC2s in apo form, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
sitting-drop method, hanging-drop vapour-diffusion method, at room temperature
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Rv0864, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kanaujia, S.P.; Jeyakanthan, J.; Nakagawa, N.; Balasubramaniam, S.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Sekar, K.
Structures of apo and GTP-bound molybdenum cofactor biosynthesis protein MoaC from Thermus thermophilus HB8
Acta Crystallogr. Sect. D
66
821-833
2010
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Yoshida, H.; Yamada, M.; Kuramitsu, S.; Kamitori, S.
Structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472)
Acta Crystallogr. Sect. F
64
589-592
2008
Sulfurisphaera tokodaii (Q975D5), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q975D5)
brenda
Rieder, C.; Eisenreich, W.; O'Brien, J.; Richter, G.; Gtze, E.; Boyle, P.; Blanchard, S.; Bacher, A.; Simon, H.
Rearrangement reactions in the biosynthesis of molybdopterin - an NMR study with multiply 13C/15N labelled precursors
Eur. J. Biochem.
255
24-36
1998
Escherichia coli
brenda
Wuebbens, M.M.; Rajagopalan, K.V.
Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies
J. Biol. Chem.
270
1082-1087
1995
Escherichia coli
brenda
Srivastava, S.; Srivastava, V.K.; Arora, A.; Pratap, J.V.
Overexpression, purification, crystallization and preliminary X-ray analysis of putative molybdenum cofactor biosynthesis protein C (MoaC2) from Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
68
687-691
2012
Mycobacterium tuberculosis (P9WJR7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJR7), Mycobacterium tuberculosis H37Rv
brenda
Srivastava, V.K.; Srivastava, S.; Srivastava, S.; Arora, A.; Pratap, J.V.
Structural insights into putative molybdenum cofactor biosynthesis protein C (MoaC2) from Mycobacterium tuberculosis H37Rv
PLoS ONE
8
e58333
2013
Mycobacterium tuberculosis (P9WJR7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJR7), Mycobacterium tuberculosis H37Rv
brenda
Hover, B.M.; Tonthat, N.K.; Schumacher, M.A.; Yokoyama, K.
Mechanism of pyranopterin ring formation in molybdenum cofactor biosynthesis
Proc. Natl. Acad. Sci. USA
112
6347-6352
2015
Escherichia coli (P0A738)
brenda
Gray, T.A.; Nicholls, R.D.
Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames
RNA
6
928-936
2000
Homo sapiens (Q9NZB8)
brenda
Hover, B.M.; Lilla, E.A.; Yokoyama, K.
Mechanistic investigation of cPMP synthase in molybdenum cofactor biosynthesis using an uncleavable substrate analogue
Biochemistry
54
7229-7236
2015
Escherichia coli
brenda
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