Literature summary for 4.3.99.3 extracted from

Dowling, D.P.; Bruender, N.A.; Young, A.P.; McCarty, R.M.; Bandarian, V.; Drennan, C.L.
Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism (2014), Nat. Chem. Biol., 10, 106-112.

Search for more literature for 4.3.99.3

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)	Burkholderia multivorans

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified His6-tagged enzyme in complex with substrate 6-carboxy-5,6,7,8-tetrahydropterin and cofactor S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.2-2.6 A resolution	Burkholderia multivorans

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	the enzyme uses a bound [4Fe-4S]+ cluster to catalyze the reductive cleavage of S-adenosyl-L-methionine cofactor to generate methionine, a single [4Fe-4S] cluster per monomer. The cluster-binding motifs of each monomer are located at opposite ends of the dimer molecule, of the Fe atoms from the cluster are coordinated by three cysteine residues from the CX14CXPhiC motif. The remaining unique Fe binds the alpha-amino and alpha-carboxyl groups of S-adenosyl-L-methionine, which adopts an anti orientation about the glycosidic bond	Burkholderia multivorans
Mg2+	dependent on, the ligand environment about Mg2+ is pseudo-octahedral, with three water ligands, the substrate C4 carbonyl and C6 carboxylate oxygens, and the hydroxyl of T51	Burkholderia multivorans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
6-carboxy-5,6,7,8-tetrahydropterin	Burkholderia multivorans	-	7-carboxy-7-carbaguanine + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Burkholderia multivorans	A0A0H3KB22	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration	Burkholderia multivorans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6-carboxy-5,6,7,8-tetrahydropterin	-	Burkholderia multivorans	7-carboxy-7-carbaguanine + NH3	-	?
6-carboxy-5,6,7,8-tetrahydropterin	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	Burkholderia multivorans	7-carboxy-7-carbaguanine + NH3	-	?
additional information	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	Burkholderia multivorans	?	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Burkholderia multivorans

Synonyms

Synonyms	Comment	Organism
CDG synthase	-	Burkholderia multivorans
queE	-	Burkholderia multivorans

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Burkholderia multivorans

Cofactor

Cofactor	Comment	Organism	Structure
additional information	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	Burkholderia multivorans
S-adenosyl-L-methionine	the binding site is conserved despite modified enzyme fold	Burkholderia multivorans

General Information

General Information	Comment	Organism
evolution	QueE is a member of the radical S-adenosyl-L-methionine superfamily, it varies from the other members in that it contains a hypermodified (beta6/alpha3) protein core and an expanded cluster-binding motif CX14CX2C, structure comparisons, overview	Burkholderia multivorans
metabolism	the enzyme catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin to 7-carboxy-7-carbaguanine in the third step of the biosynthetic pathway to all 7-deazapurines. 7-Carboxy-7-carbaguanine is the first 7-deazapurine in the biosynthetic pathway and likely the precursor to all naturally occurring 7-deazapurine containing molecules	Burkholderia multivorans
additional information	substrate binding generates a metal-binding site	Burkholderia multivorans

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Release 2023.1 (January 2023)