4.3.99.3: 7-carboxy-7-deazaguanine synthase
This is an abbreviated version!
For detailed information about 7-carboxy-7-deazaguanine synthase, go to the full flat file.
Word Map on EC 4.3.99.3
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4.3.99.3
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s-adenosyl-l-methionine
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radical-mediated
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adomet
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5\'-deoxyadenosyl
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7-deazapurine
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flavodoxin
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burkholderia
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dithionite
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sam-dependent
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pyrrolopyrimidine
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multivorans
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cluster-binding
- 4.3.99.3
- s-adenosyl-l-methionine
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radical-mediated
- adomet
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5\'-deoxyadenosyl
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7-deazapurine
- flavodoxin
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burkholderia
- dithionite
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sam-dependent
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pyrrolopyrimidine
- multivorans
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cluster-binding
Reaction
Synonyms
7-carboxy-7-carbaguanine synthase, BsQueE, CDG synthase, queE, ToyC
ECTree
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Substrates Products
Substrates Products on EC 4.3.99.3 - 7-carboxy-7-deazaguanine synthase
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REACTION DIAGRAM
7-carboxy-7-carbaguanine + NH3
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
the enzyme catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
the enzyme catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
the substrate binds perpendicular to the [4Fe-4S]-bound S-adenosyl-L-methionine cofactor, exposing its C6 hydrogen atom for abstraction and generating the binding site for Mg2+, which directly coordinates to the substrate. Substrate binding generates a metal-binding site
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
the key ring-contraction step involves a bridged intermediate rather than a ring-opening one. For the QueE-Mg2+ system, the elimination of ammonia is calculated to be rate limiting, determined by investigation at an atomistic level by using the combined quantum mechanics and molecular mechanics method
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
the key ring-contraction step involves a bridged intermediate rather than a ring-opening one. For the QueE-Mg2+ system, the elimination of ammonia is calculated to be rate limiting, determined by investigation at an atomistic level by using the combined quantum mechanics and molecular mechanics method
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?
6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
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7-carboxy-7-deazaguanine + NH3
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6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-deazaguanine + NH3
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substrate from a coupled reaction with Escherichia coli CPH4 synthase
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under reducing conditions that would promote the reductive cleavage of S-adenosyl-L-methionine, 6-carboxypterin is turned over to 6-deoxyadenosylpterin, presumably by radical addition of the 5'-deoxyadenosine followed by oxidative decarboxylation to the product. In the absence of the strong reductant, dithionite, the carboxylate of 6-carboxypterin is esterified to generate 6-carboxypterin-5'-deoxyadenosyl ester
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6-carboxypterin
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under reducing conditions that would promote the reductive cleavage of S-adenosyl-L-methionine, 6-carboxypterin is turned over to 6-deoxyadenosylpterin, presumably by radical addition of the 5'-deoxyadenosine followed by oxidative decarboxylation to the product. In the absence of the strong reductant, dithionite, the carboxylate of 6-carboxypterin is esterified to generate 6-carboxypterin-5'-deoxyadenosyl ester
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the enzyme uses a bound [4Fe-4S]+ cluster to catalyze the reductive cleavage of S-adenosyl-L-methionine cofactor to generate methionine and a 5'-deoxyadenosyl radical, which initiates enzymatic transformations requiring H-atom abstraction
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additional information
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the enzyme uses a bound [4Fe-4S]+ cluster to catalyze the reductive cleavage of S-adenosyl-L-methionine cofactor to generate methionine and a 5'-deoxyadenosyl radical, which initiates enzymatic transformations requiring H-atom abstraction. To initiate radical chemistry, all AdoMet radical enzymes require the one-electron reduction of the [4Fe-4S] cluster. This electron is typically supplied by a flavodoxin. For the Burkholderia multivorans enzyme, more product is generated using the chemical reductant dithionite
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additional information
?
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the enzyme uses a bound [4Fe-4S]+ cluster to catalyze the reductive cleavage of S-adenosyl-L-methionine cofactor to generate methionine and a 5'-deoxyadenosyl radical, which initiates enzymatic transformations requiring H-atom abstraction. To initiate radical chemistry, all AdoMet radical enzymes require the one-electron reduction of the [4Fe-4S] cluster. This electron is typically supplied by a flavodoxin. For the Burkholderia multivorans enzyme, more product is generated using the chemical reductant dithionite
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?