Information on EC 4.1.99.18 - cyclic pyranopterin phosphate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.1.99.18
-
RECOMMENDED NAME
GeneOntology No.
cyclic pyranopterin phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GTP = cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
-
-
-
GTP = cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
the N-terminal [4Fe-4S] cluster is likely to be responsible for the reductive cleavage of SAM to the 5'-deoxyadenosyl radical and L-methionine and the second cluster binds to N1 of GTP. Upon generation of the 5'-deoxyadenosyl radical, GTP is transformed into (2-amino-7-hydroxy-4,6-dioxo-4,5,5a,6,7,8,9a,10-octahydro-3H-pyrano[3,2-g]pteridin-8-yl)methyl triphosphate via a complex rearrangement reaction where the C8 atom of the purine is inserted between the C2' and the C3' atoms of the ribose moiety. MoaC then catalyzes the intramolecular cyclization reaction of (2-amino-7-hydroxy-4,6-dioxo-4,5,5a,6,7,8,9a,10-octahydro-3H-pyrano[3,2-g]pteridin-8-yl)methyl triphosphate to (2-amino-7-hydroxy-4,6-dioxo-4,5,5a,6,7,8,9a,10-octahydro-3H-pyrano[3,2-g]pteridin-8-yl)methyl triphosphate which is oxidized to 2-amino-6-(2,5-dihydroxy-2-oxido-1,3,2-dioxaphosphinane-4-carbonyl)pteridin-4(3H)-one prior to analysis because of the instability of (2-amino-7-hydroxy-4,6-dioxo-4,5,5a,6,7,8,9a,10-octahydro-3H-pyrano[3,2-g]pteridin-8-yl)methyl triphosphate
-
GTP = cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
proposed mechanism for the MoaA/MoaC-catalyzed reaction, detailed overview. MoaA/MoaC catalyzes a remarkable rearrangement reaction in which the C8 of GTP is inserted into the ribose C2'-C3' bond, several radical reaction intermediates, mass spectrometric analysis
-
GTP = cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
mechanisms proposed for the first step of the Moco biosynthesis pathway, overview
P9WJR7
PATHWAY
KEGG Link
MetaCyc Link
molybdenum cofactor biosynthesis
-
Folate biosynthesis
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
GTP 8,9-lyase (cyclic pyranopterin monophosphate-forming)
The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). The enzyme MoaA from bacteria and the human enzyme MOCS1A each contain two oxygen-sensitive FeS clusters. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. In bacteria, the reaction is catalysed by MoaA and requires the action of MoaC. The latter protein is equivalent to the C-terminal domain of the eukaryotic enzyme MOCS1A which does not need further protein components to perform the reaction.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
MoaA
-
-
-
-
MoaA
-
gene name
MoaC
-
-
-
-
MoaC
Q975D5
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
MoaC
Sulfolobus tokodaii 7
Q975D5
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
Moco-biosynthesis protein
O66472
-
Moco-biosynthesis protein
P9WJR7
-
Moco-biosynthesis protein
Q5SLF2
-
MOCS1A
-
-
-
-
MOCS1A
-
-
MOCS1B
-
-
MogA
O66472
-
molybdenum cofactor biosynthesis protein 1
-
-
-
-
molybdenum cofactor biosynthesis protein C
P9WJR7
-
molybdenum cofactor biosynthetic enzyme
-
-
molybdenum-cofactor biosynthesis protein
O66472
-
molybdenum-cofactor biosynthesis protein
Q5SLF2
-
ST0472
Q975D5
-
ST0472
Sulfolobus tokodaii 7
Q975D5
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
mog gene, aq_061
UniProt
Manually annotated by BRENDA team
MoaC2; gene Rv0864
UniProt
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
SwissProt
Manually annotated by BRENDA team
gene TTHA0341
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
MoaA is a member of the radical-SAM superfamily of proteins and harbors two [4Fe-4S]2+1+ clusters
evolution
-
MoaA is a member of the S-adenosylmethionine (SAM)-dependent radical enzyme superfamily
evolution
P9WJR7
MoaA belongs to the S-adenosyl-L-methionine-dependent radical enzyme superfamily, members of which catalyse the formation of protein or substrate radicals by reductive cleavage of SAM by a [4Fe-4S] cluster
metabolism
P9WJR7
the enzymes is involved in the molybdenum cofactor (Moco) biosynthesis pathway. Together with MoaA, MoaC is involved in the conversion of guanosine triphosphate (GTP) to precursor Z, the first step in Moco synthesis
metabolism
-
MoaA and MoaC catalyze the first step in molybdopterin biosynthesis. This reaction involves a complex rearrangement in which C8 of guanosine triphosphtate is inserted between the C2' and the C3' carbons of the ribose
metabolism
-
the enzyme catalyzes teh first step of molybdenum cofactor biosynthesis, the formation of cyclic pyranopterin monophosphate, cPMP
metabolism
-
MoaA and MoaC together catalyze the first step in molybdopterin biosynthesis, converting GTP to cyclic pyranopterin monophosphate
physiological function
-
the formation of the cyclic pyranopterin monophosphate from GTP is an early step in the biosynthesis of the molybdenum cofactor. It is catalyzed by MaoA and requires the action of MoaC
physiological function
Q975D5, -
the formation of the cyclic pyranopterin monophosphate from GTP is an early step in the biosynthesis of the molybdenum cofactor. It is catalyzed by MaoA and requires the action of MoaC
physiological function
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
Sulfolobus tokodaii 7
-
the formation of the cyclic pyranopterin monophosphate from GTP is an early step in the biosynthesis of the molybdenum cofactor. It is catalyzed by MaoA and requires the action of MoaC
-
metabolism
P9WJR7
the formation of precursor Z from guanosine triphosphate in the Molybdenum cofactor (Moco) biosynthesis pathway is catalysed by two enzymes, MoaA and MoaC
additional information
-, O66472
detailed structure analysis, docking, and molecular-dynamics simulations, active site structure and structure comparisons, overview
additional information
Q5SLF2, -
detailed structure analysis, docking, and molecular-dynamics simulations, active site structure and structure comparisons, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
reaction of MoaC
-
-
?
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
reaction of MoaC, which is responsible for the formation of the cyclic phosphate
NMR spectroscopy product analysis
-
?
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
reaction of MOCS1B, responsible for the formation of the cyclic phosphate
NMR spectroscopy product analysis
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
P65388
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
P65388
the reaction is catalysed by MoaA and requires the action of MoaC
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the reaction is catalyzed by the S-adenosyl-L-methionine-dependent enzyme MoaA and the accessory protein MoaC. This reaction involves the radical-initiated intramolecular rearrangement of the guanine C8 atom
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
-
-
?
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
show the reaction diagram
-
reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC
-
-
?
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
show the reaction diagram
-
reaction of MoaA
NMR spectroscopy product analysis
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-, P9WJR7
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
P9WJR7
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
MoaA cleaves GTP by a radical mechanism, a 5'-desoxyadenosyl radical is generated from S-adenosyl-L-methionine at the N-terminal cluster facilitating hydrogen abstraction at either the C8 of the guanine or the C2' or C3' atoms of the ribose. Insertion of the formyl group between the ribose C2' and C3' carbons might also require radical mediation. MoaC is involved in the cleavage of the dihydropyrazine-type intermediate pyrophosphate group and formation of the cPMP cyclic phosphate group
-
-
?
additional information
?
-
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
-
additional information
?
-
Q975D5, -
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
-
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
-
-
-
additional information
?
-
P9WJR7
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
?
-
Q5SLF2, -
binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview
-
-
-
additional information
?
-
-, O66472
binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview
-
-
-
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
-
-
-
additional information
?
-
P9WJR7
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
?
-
Sulfolobus tokodaii 7
Q975D5
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
reaction of MoaC
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
P65388
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
show the reaction diagram
-
reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-, P9WJR7
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
P9WJR7
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
MoaA cleaves GTP by a radical mechanism, a 5'-desoxyadenosyl radical is generated from S-adenosyl-L-methionine at the N-terminal cluster facilitating hydrogen abstraction at either the C8 of the guanine or the C2' or C3' atoms of the ribose. Insertion of the formyl group between the ribose C2' and C3' carbons might also require radical mediation. MoaC is involved in the cleavage of the dihydropyrazine-type intermediate pyrophosphate group and formation of the cPMP cyclic phosphate group
-
-
?
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
-
-
-
additional information
?
-
P9WJR7
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)
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
iron-sulfur centre
Q44118
the enzyme contains iron-sulfur centres
iron-sulfur centre
-
contains two oxygen-sensitive FeS clusters, each coordinated by three cysteine residues. A redox-active [4Fe-4S]2+cluster is ligated by an N-terminal CX3CX2C motif as is the case with all other D-adenosylmethionione-dependent radical enzymes investigated thus far. A C-terminal CX2CX13C motif that is unique to MOCS1A and its orthologs primarily ligates a [3Fe-4S] cluster. MOCS1A can be reconstituted in vitro under anaerobic conditions to yield a form containing two [4Fe-4S]2+clusters. The N-terminal [4Fe-4S]2+cluster is rapidly degraded by oxygen via a semistable [2Fe-2S]2+ cluster intermediate, and the C-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen to yield a semistable [3Fe-4S] cluster intermediate
iron-sulfur centre
-
binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate
iron-sulfur centre
-
MoaA harbors an N-terminal [4Fe-4S] cluster, which is involved in the reductive cleavage of S-adenosyl-L-methionine and generates a 5'-deoxyadenosyl radical, and a C-terminal [4Fe-4S] cluster presumably involved in substrate binding andor activation. MoaA binds 5'-GTP with high affinity and interacts through its C-terminal [4Fe-4S] cluster with the guanine N1 and N2 atoms
S-adenosyl-L-methionine
-
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
S-adenosyl-L-methionine
-
MoaA is a radical S-adenosylmethionine (SAM) enzyme
S-adenosyl-L-methionine
-
MoaAis a radical S-adenosyl-L-methionine (SAM) enzyme. S-adenosyl-L-methionine serves as the free radical initiator and undergoes cleavage to methionine and a 5'-deoxyadenosyl radical that in turn initiates radical formation of substrate molecules or of glycyl residues within the target enzymes to activate them for radical-based chemistry. The source of the electron required for the cleavage of SAM is a reduced form of a conserved FeS cluster within the protein
S-adenosyl-L-methionine
-
MoaA as a radical S-adenosyl-L-methionine enzyme
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
MoaA harbors two [4Fe-4S]2+,1+ clusters, the N-terminal [4Fe-4S] cluster is likely to be responsible for the reductive cleavage of SAM to the 5'-deoxyadenosyl radical and L-methionine and the second cluster binds to N1 of GTP
Fe2+
-
MoaA contains two oxygen-sensitive [4Fe-4S] clusters, one typical for S-adenosylmethionine-dependent radical enzymes at the N-terminus and an additional C-terminal cluster unique to MoaA proteins
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
iron-sulfur centre
Q44118
the enzyme contains iron-sulfur centres
iron-sulfur centre
-
guanine N1 binds to [4Fe-4S] cluster II
iron-sulfur centre
-
contains two oxygen-sensitive FeS clusters, each coordinated by only three cysteine residues. A redox-active [4Fe-4S]2+,+cluster is ligated by an N-terminal CX3CX2C motif as is the case with all other D-adenosylmethionione-dependent radical enzymes investigated thus far. A C-terminal CX2CX13C motif that is unique to MOCS1A and its orthologs primarily ligates a [3Fe-4S]0 cluster. MOCS1A can be reconstituted in vitro under anaerobic conditions to yield a form containing two [4Fe-4S]2+clusters. The N-terminal [4Fe-4S]2+cluster is rapidly degraded by oxygen via a semistable [2Fe-2S]2+ cluster intermediate, and the C-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen to yield a semistable [3Fe-4S]0 cluster intermediate
iron-sulfur centre
-
binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate
iron-sulfur centre
-
MoaA harbors an N-terminal [4Fe-4S] cluster, which is involved in the reductive cleavage of S-adenosyl-L-methionine and generates a 5'-deoxyadenosyl radical, and a C-terminal [4Fe-4S] cluster presumably involved in substrate binding andor activation. MoaA binds 5'-GTP with high affinity and interacts through its C-terminal [4Fe-4S] cluster with the guanine N1 and N2 atoms
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
MoaC protein
-
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
-
MoaC protein
-
formation cyclic pyranopterin monophosphate by MoaA requires the action of MoaC protein
-
MoaC protein
-
the reaction is catalyzed by the S-adenosylmethionine-dependent enzyme MoaA and the accessory protein MoaC
-
additional information
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
additional information
Q975D5, -
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00006
-
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
-
pH 7.6, 25°C, MOCS1B
-
0.00079
-
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
-
pH 7.6, 25°C, MoaC
-
additional information
-
additional information
-, O66472
molecular dynamics and docking studies with several small molecules, including substrate and product, binding affinities towards AaMogA, overview
-
additional information
-
additional information
Q5SLF2, -
molecular dynamics and docking studies with several small molecules, including substrate and product, binding affinities towards TtMogA, overview
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
-
assay at, MOCS1B
7.6
-
-
assay at, MoaA and MoaC
9
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at
25
-
-
assay at, MOCS1B
25
-
-
assay at, MoaA and MoaC
PDB
SCOP
CATH
ORGANISM
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain NCTC 8325)
Staphylococcus aureus (strain NCTC 8325)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41000
-
-
monomer, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da), gel filtration
82000
-
-
homodimer, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da), gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
P9WJR7
x * 17500, MoaC2
dimer
-
2 * 42000, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da)
dimer
P9WJR7
2 * 17500, MoaC2 functional form
hexamer
Q975D5, -
-
hexamer
P9WJR7
MoaC2 mainly forms hexamers, which are not functional
hexamer
Sulfolobus tokodaii 7
-
-
-
monomer
-
1 * 42000, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da)
additional information
-, O66472
homology structure comparisons for identification of residues involved in protein oligomerization, overview
additional information
Q5SLF2, -
homology structure comparisons for identification of residues involved in protein oligomerization, overview
additional information
P9WJR7
tertiary and quaternary structures of MoaC2, detailed overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant enzyme, mixing of 0.001 ml of 24 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 0.2 M NaCl, with 0.001 ml of reservoir solution containing 40% v/v PEG 600, 100 mM CHES buffer, pH 9.5, or 0.2 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, 25% w/v PEG 3350, 1 week, two different crystal forms, X-ray diffraction structure determination and analysis at 1.7-1.9 A resolution, molecular replacement method
-, O66472
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
P9WJR7
purified recombinant MoaC2s in apo form, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
P9WJR7
crystal structure of wild-type MoaA, MoaA-R17A/R266A/R268A and MoaA in complex with 5'-GTP2.35 A resolution
-
crystals are grown under anaerobic conditions, hanging drop vapor diffusion technique, crystals belong to space group P2(1)2(1)2(1) with cell dimensions of a = 48.1, b = 102.4, and c = 191.2 A and contain two molecules per asymmetric unit, structures of MoaA in the apo-state (2.8 A) and in complex with S-adenosyl-L-methionine (2.2 A)
-
sitting-drop method, hanging-drop vapour-diffusion method, at room temperature
Q975D5, -
GTP-bound crystal structure
-
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.64 A resolution, molecular replacement method
Q5SLF2, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by two different times of gel filtration and anion exchange chromatography, followed by gel filtration and hydroxyapatite chromatography, and a last step of gel filtration
-, O66472
recombinant MOCS1B from Escherichia coli strain BL21(DE3) by streptomycin sulfate and ammonium sulfate precipitation steps, nickel affinity chromatography, gell filtration, and ultrafiltration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography and gel filtration
P9WJR7
purified under anaerobic conditions
-
recombinant enzyme
Q5SLF2, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene mog, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
-, O66472
expression in Escherichia coli
-
MOCS1B overexpression in Escherichia coli strain BL21(DE3)
-
gene Rv0864, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
P9WJR7
expressed as His-tagged proteins in Escherichia coli
-
gene mogA, phylogenetic tree, recombinant expression
Q5SLF2, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme expression is downregulated by 3times in the nutrient starvation model for Mycobacterium tuberculosis
P9WJR7
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C24S/C28S/C31S
-
the mutant does not contain the catalytic S-adenosyl-L-methionine-binding cluster I
N124A/N165A
-
mutation reduces binding of 5'-GTP
R17A
-
complete loss of activity
R17A/R266A/R268A
-
complete loss of activity
R192A
-
80% loss of activity
R266A
-
complete loss of activity
R268A
-
complete loss of activity
R71A
-
80% loss of activity
S126A
-
mutant enzyme with low activity
T73A
-
mutant enzyme with low activity
Y30A
-
mutant enzyme with low activity