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GTP + S-adenosyl-L-methionine + reduced electron acceptor = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
GTP + S-adenosyl-L-methionine + reduced electron acceptor = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
-
GTP + S-adenosyl-L-methionine + reduced electron acceptor = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
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
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GTP + S-adenosyl-L-methionine + reduced electron acceptor = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
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
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(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
GMP[CH2]PP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine-P[CH2]PP + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
GTP
cyclic pyranopterin phosphate + diphosphate
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
additional information
?
-
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
-
reaction of MOCS1B, responsible for the formation of the cyclic phosphate
NMR spectroscopy product analysis
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?
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
-
reaction of MoaC
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-
?
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
-
reaction of MoaC, which is responsible for the formation of the cyclic phosphate
NMR spectroscopy product analysis
-
?
GMP[CH2]PP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine-P[CH2]PP + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
substrate has a methylene bridge in place of an oxygen between the alpha and bveta phosphate groups
product has a methylene bridge in place of an oxygen between the alpha and beta phosphate groups and product is an uncleavable substrate analogue of cyclic pyranopterin monophosphate synthase accessory protein MoaC
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?
GMP[CH2]PP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine-P[CH2]PP + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
substrate has a methylene bridge in place of an oxygen between the alpha and bveta phosphate groups
product has a methylene bridge in place of an oxygen between the alpha and beta phosphate groups and product is an uncleavable substrate analogue of cyclic pyranopterin monophosphate synthase accessory protein MoaC
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?
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
-
reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC
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-
?
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
-
reaction of MoaA
NMR spectroscopy product analysis
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?
GTP
cyclic pyranopterin phosphate + diphosphate
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-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
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-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
-
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
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?
GTP
cyclic pyranopterin phosphate + diphosphate
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?
GTP
cyclic pyranopterin phosphate + diphosphate
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
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-
?
GTP
cyclic pyranopterin phosphate + diphosphate
-
-
-
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?
GTP
cyclic pyranopterin phosphate + diphosphate
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
the reaction is catalysed by MoaA and requires the action of MoaC
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?
GTP
cyclic pyranopterin phosphate + diphosphate
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
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?
GTP
cyclic pyranopterin phosphate + diphosphate
-
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
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?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
pyranopterin triphosphate is formed as a by-product, the amount is 0.4Ā3% of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine formed
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?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
pyranopterin triphosphate is formed as a by-product, the amount is 0.4Ā3% of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine formed
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?
additional information
?
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binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview
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-
?
additional information
?
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binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview
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?
additional information
?
-
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binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview
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-
?
additional information
?
-
binding energetics of substrates and compounds, e.g. GTP, GMP, GDP, AMP, ADP, ATP, and molydopterin, docking study, overview
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-
?
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(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
cyclic pyranopterin phosphate + diphosphate
-
reaction of MoaC
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-
?
GTP
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
-
reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC
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-
?
GTP
cyclic pyranopterin phosphate + diphosphate
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
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
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
-
-
-
-
?
GTP
cyclic pyranopterin phosphate + diphosphate
-
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
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-
?
GTP
cyclic pyranopterin phosphate + diphosphate
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
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?
GTP
cyclic pyranopterin phosphate + diphosphate
-
-
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?
GTP
cyclic pyranopterin phosphate + diphosphate
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
?
GTP + S-adenosyl-L-methionine + reduced electron acceptor
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + oxidized electron acceptor
-
-
-
?
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malfunction
cyclic pyranopterin monophosphate (cPMP) is strongly decreased in cnx2 mutants. Phenotype of T-DNA insertion mutant line cnx2-1, the cnx2-1 knockout is seedling-lethal but growth is rescued by ammonia, overview. Mutant xd22 has a mutation in CNX2 affecting the proximal FeS cluster loop. With hypoxanthine as a substrate, no activity is detectable in leaves from cnx2-2 plants. Nitrate reductase activity in leaf extract from cnx2-2 is 55% compared to wild-type values. Genetic complementation and strongly decreased activities of Moco enzymes show that the mutation in xd22 (R88Q) is located in CNX2, line cnx2-2, encoding the first step in Moco biosynthesis. The cnx2-2 mutation is not a knockout allele and growth is rescued by ammonia. Crosses between heterozygous cnx2-1 CNX2 and homozygous cnx2-2 plants give F1 offspring in two phenotype categories: seedlings with wild-type appearance corresponding to cnx2-1 CNX2 and small chlorotic seedlings that are genotyped as cnx2-1 cnx2-2
malfunction
-
cyclic pyranopterin monophosphate (cPMP) is strongly decreased in cnx2 mutants. Phenotype of T-DNA insertion mutant line cnx2-1, the cnx2-1 knockout is seedling-lethal but growth is rescued by ammonia, overview. Mutant xd22 has a mutation in CNX2 affecting the proximal FeS cluster loop. With hypoxanthine as a substrate, no activity is detectable in leaves from cnx2-2 plants. Nitrate reductase activity in leaf extract from cnx2-2 is 55% compared to wild-type values. Genetic complementation and strongly decreased activities of Moco enzymes show that the mutation in xd22 (R88Q) is located in CNX2, line cnx2-2, encoding the first step in Moco biosynthesis. The cnx2-2 mutation is not a knockout allele and growth is rescued by ammonia. Crosses between heterozygous cnx2-1 CNX2 and homozygous cnx2-2 plants give F1 offspring in two phenotype categories: seedlings with wild-type appearance corresponding to cnx2-1 CNX2 and small chlorotic seedlings that are genotyped as cnx2-1 cnx2-2
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metabolism
molybdenum cofactor (Moco) biosynthesis starts with the condensation of GTP into cyclic pyranopterin monophosphate (cPMP) by the consecutive action of GTP 3',8-cyclase and cPMP synthase, encoded by CNX2 and CNX3 in plants, respectively, pathways for FeS cluster assembly and Moco biosynthesis in Arabidopsis thaliana, overview
metabolism
-
the enzyme MoaA catalyzes the fist step of molybdenum cofactor (Moco) biosynthesis
metabolism
-
molybdenum cofactor (Moco) biosynthesis starts with the condensation of GTP into cyclic pyranopterin monophosphate (cPMP) by the consecutive action of GTP 3',8-cyclase and cPMP synthase, encoded by CNX2 and CNX3 in plants, respectively, pathways for FeS cluster assembly and Moco biosynthesis in Arabidopsis thaliana, overview
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metabolism
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the enzyme MoaA catalyzes the fist step of molybdenum cofactor (Moco) biosynthesis
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physiological function
the GG motif is essential for the activity of MoaA to produce (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate from GTP, and synthetic peptides corresponding to the C-terminal region of wild-type MoaA rescue the GTP 3',8-cyclase activity of the GG-motif mutants. The C-terminal tail containing the GG motif interacts with the SAM-binding pocket of MoaA, and is essential for the binding of SAM and subsequent radical initiation
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
physiological function
-
the MoaA protein is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate in the fist step of molybdenum cofactor (Moco) biosynthesis
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
-
physiological function
-
the GG motif is essential for the activity of MoaA to produce (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate from GTP, and synthetic peptides corresponding to the C-terminal region of wild-type MoaA rescue the GTP 3',8-cyclase activity of the GG-motif mutants. The C-terminal tail containing the GG motif interacts with the SAM-binding pocket of MoaA, and is essential for the binding of SAM and subsequent radical initiation
-
physiological function
-
the MoaA protein is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate in the fist step of molybdenum cofactor (Moco) biosynthesis
-
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C24S/C28S/C31S
-
the mutant does not contain the catalytic S-adenosyl-L-methionine-binding cluster I
D198A
mutation in GG motif, decrease in affinity for S-adenosine-L-methionine
G339A
mutation in GG motif, loss of activity
G340A
mutation in GG motif, loss of activity
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
D198A
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mutation in GG motif, decrease in affinity for S-adenosine-L-methionine
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G339A
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mutation in GG motif, loss of activity
-
G340A
-
mutation in GG motif, loss of activity
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R88Q
mutant xd22 has a mutation in CNX2 affecting the proximal FeS cluster loop. Complementation of the cnx2-2 phenotype by a genomic fragment including the promoter region from position -1224 and UTRs, amplified by PCR. Mutant cnx2-2 plants are transformed using Agrobacterium tumefaciens strain GV3101. The cnx2-2 mutation is not a knockout allele and growth is rescued by ammonia. Crosses between heterozygous cnx2-1 CNX2 and homozygous cnx2-2 plants give F1 offspring in two phenotype categories: seedlings with wild-type appearance corresponding to cnx2-1 CNX2 and small chlorotic seedlings that are genotyped as cnx2-1 cnx2-2
R88Q
-
mutant xd22 has a mutation in CNX2 affecting the proximal FeS cluster loop. Complementation of the cnx2-2 phenotype by a genomic fragment including the promoter region from position -1224 and UTRs, amplified by PCR. Mutant cnx2-2 plants are transformed using Agrobacterium tumefaciens strain GV3101. The cnx2-2 mutation is not a knockout allele and growth is rescued by ammonia. Crosses between heterozygous cnx2-1 CNX2 and homozygous cnx2-2 plants give F1 offspring in two phenotype categories: seedlings with wild-type appearance corresponding to cnx2-1 CNX2 and small chlorotic seedlings that are genotyped as cnx2-1 cnx2-2
-
additional information
generation of cnx2 mutants by T-DNA insertion, line cnx2-1, and point mutation, line cnx2-2. Mutation mapping by whole genome sequencing, phenotype analyses
additional information
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generation of cnx2 mutants by T-DNA insertion, line cnx2-1, and point mutation, line cnx2-2. Mutation mapping by whole genome sequencing, phenotype analyses
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additional information
-
deletion of central components of the ISC system in addition to IscS leads to an overall decrease in Fe-S cluster enzyme and molybdoenzyme activity in addition to a decrease in the number of Fe-S-dependent thiomodifications of tRNA, based on the fact that some proteins involved in Moco biosynthesis and tRNA thiolation are Fe-S-dependent. Complementation of the ISC deficient strains with the suf operon restores the activity of Fe-S-containing proteins, including the MoaA protein, which is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate in the fist step of Moco biosynthesis
additional information
-
deletion of central components of the ISC system in addition to IscS leads to an overall decrease in Fe-S cluster enzyme and molybdoenzyme activity in addition to a decrease in the number of Fe-S-dependent thiomodifications of tRNA, based on the fact that some proteins involved in Moco biosynthesis and tRNA thiolation are Fe-S-dependent. Complementation of the ISC deficient strains with the suf operon restores the activity of Fe-S-containing proteins, including the MoaA protein, which is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate in the fist step of Moco biosynthesis
-
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Menendez, C.; Siebert, D.; Brandsch, R.
MoaA of Arthrobacter nicotinovorans pAO1 involved in Mo-pterin cofactor synthesis is an Fe-S protein
FEBS Lett.
391
101-103
1996
Paenarthrobacter nicotinovorans (Q44118)
brenda
Lees, N.S.; Hänzelmann, P.; Hernandez, H.L.; Subramanian, S.; Schindelin, H.; Johnson, M.K.; Hoffman, B.M.
ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications
J. Am. Chem. Soc.
131
9184-9185
2009
Staphylococcus aureus
brenda
Hänzelmann, P.; Hernandez, H.L.; Menzel, C.; Garcia-Serres, R.; Huynh, B.H.; Johnson, M.K.; Mendel, R.R.; Schindelin, H.
Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis
J. Biol. Chem.
279
34721-34732
2004
Homo sapiens
brenda
Hänzelmann, P.; Schindelin, H.
Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
Proc. Natl. Acad. Sci. USA
101
12870-12875
2004
Staphylococcus aureus (P65388)
brenda
Hänzelmann, P.; Schindelin, H.
Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism
Proc. Natl. Acad. Sci. USA
103
6829-6834
2006
Staphylococcus aureus (P65388)
brenda
Kanaujia, S.P.; Jeyakanthan, J.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Sekar, K.
Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms
Acta Crystallogr. Sect. F
67
2-16
2011
Aquifex aeolicus (O66472), Aquifex aeolicus, Thermus thermophilus (Q5SLF2), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SLF2)
brenda
Mehta, A.P.; Hanes, J.W.; Abdelwahed, S.H.; Hilmey, D.G.; Haenzelmann, P.; Begley, T.P.
Catalysis of a new ribose carbon-insertion reaction by the molybdenum cofactor biosynthetic enzyme MoaA
Biochemistry
52
1134-1136
2013
Bacteria
brenda
Iobbi-Nivol, C.; Leimkuehler, S.
Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli
Biochim. Biophys. Acta
1827
1086-1101
2013
Escherichia coli
brenda
Mehta, A.P.; Abdelwahed, S.H.; Begley, T.P.
Molybdopterin biosynthesis: trapping an unusual purine ribose adduct in the MoaA-catalyzed reaction
J. Am. Chem. Soc.
135
10883-10885
2013
Bacteria
brenda
Hover, B.M.; Loksztejn, A.; Ribeiro, A.A.; Yokoyama, K.
Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis
J. Am. Chem. Soc.
135
7019-7032
2013
Homo sapiens, Staphylococcus aureus
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
Staphylococcus aureus (P69848), Staphylococcus aureus NCTC 8325 (P69848)
brenda
Hover, B.M.; Yokoyama, K.
C-Terminal glycine-gated radical initiation by GTP 3',8-cyclase in the molybdenum cofactor biosynthesis
J. Am. Chem. Soc.
137
3352-3359
2015
Staphylococcus aureus (P65388), Staphylococcus aureus N315 (P65388)
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
Staphylococcus aureus (P69848), Staphylococcus aureus NCTC 8325 (P69848)
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), Homo sapiens
brenda
Kruse, I.; Maclean, A.E.; Hill, L.; Balk, J.
Genetic dissection of cyclic pyranopterin monophosphate biosynthesis in plant mitochondria
Biochem. J.
475
495-509
2018
Arabidopsis thaliana (Q39055), Arabidopsis thaliana Col-0 (Q39055)
brenda
Buehning, M.; Valleriani, A.; Leimkuehler, S.
The role of SufS is restricted to Fe-S cluster biosynthesis in Escherichia coli
Biochemistry
56
1987-2000
2017
Escherichia coli, Escherichia coli BW25113
brenda