4.1.99.22: GTP 3',8-cyclase
This is an abbreviated version!
For detailed information about GTP 3',8-cyclase, go to the full flat file.
Word Map on EC 4.1.99.22
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4.1.99.22
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bicistronic
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s-adenosyl-l-methionine
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s-adenosylmethionine
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pyranopterin
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monophosphate
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molybdopterin
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barrel
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auxiliary
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pterin
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epr
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adomet
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mocs2a
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gephyrin
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embodying
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xanthine
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ansme
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hexamer
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butirosin
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monoclinic
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5'-deoxyadenosine
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thermus
- 4.1.99.22
-
bicistronic
- s-adenosyl-l-methionine
- s-adenosylmethionine
-
pyranopterin
- monophosphate
- molybdopterin
-
barrel
-
auxiliary
- pterin
- epr
- adomet
-
mocs2a
-
gephyrin
-
embodying
- xanthine
- ansme
-
hexamer
- butirosin
-
monoclinic
- 5'-deoxyadenosine
-
thermus
Reaction
Synonyms
AT2G31955, cnx2, CNX2/MOCS1A, EC 4.1.99.18, MoaA, MoaC, Moco-biosynthesis protein, MOCS1A, MOCS1B, MogA, molybdenum cofactor biosynthetic enzyme, molybdenum-cofactor biosynthesis protein
ECTree
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Cofactor
Cofactor on EC 4.1.99.22 - GTP 3',8-cyclase
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Fe-S center
CNX2/MOCS1A is an FeS enzyme depending on two Fe4S4 clusters, which are assembled by the mitochondrial FeS cluster assembly pathway
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
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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
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
iron-sulfur centre
the enzyme contains iron-sulfur centres
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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
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MoaA as a radical S-adenosyl-L-methionine enzyme
S-adenosyl-L-methionine
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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