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Literature summary for 2.6.1.B18 extracted from

  • Bon Ramos, A.; Bao, L.; Turner, B.; de Crecy-Lagard, V.; Iwata-Reuyl, D.
    QueF-Like, a Non-Homologous Archaeosine Synthase from the Crenarchaeota (2017), Biomolecules, 7, 36 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.B18

Cloned(Commentary)

Cloned (Comment) Organism
gene queF-L, recombinant overexpression of His6-tagged enzyme in Escherichia coli Pyrobaculum calidifontis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7-cyano-7-carbaguanosine15 in tRNA + NH4+ Pyrobaculum calidifontis
-
 archaeosine15 in tRNA
-
 ?
7-cyano-7-carbaguanosine15 in tRNA + NH4+ Pyrobaculum calidifontis JCM 11548
-
 archaeosine15 in tRNA
-
 ?
7-cyano-7-carbaguanosine15 in tRNA + NH4+ Pyrobaculum calidifontis VA1
-
 archaeosine15 in tRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrobaculum calidifontis A3MSP1
-
-
Pyrobaculum calidifontis JCM 11548 A3MSP1
-
-
Pyrobaculum calidifontis VA1 A3MSP1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli by heat treatment at 80°C and nickel affinity chromatography, to over 95% homogeneity Pyrobaculum calidifontis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7-cyano-7-carbaguanosine15 in tRNA + NH4+
-
 Pyrobaculum calidifontis archaeosine15 in tRNA
-
 ?
7-cyano-7-carbaguanosine15 in tRNA + NH4+
-
 Pyrobaculum calidifontis JCM 11548 archaeosine15 in tRNA
-
 ?
7-cyano-7-carbaguanosine15 in tRNA + NH4+
-
 Pyrobaculum calidifontis VA1 archaeosine15 in tRNA
-
 ?

Synonyms

Synonyms Comment Organism
ammonium:preQ0-tRNA aminotransferase UniProt Pyrobaculum calidifontis
Pcal_0221 locus name Pyrobaculum calidifontis
QueF-L
-
 Pyrobaculum calidifontis
QueF-like
-
 Pyrobaculum calidifontis

General Information

General Information Comment Organism
evolution the organism lacks an archaeosine synthase, but comprises two proteins that inversely distribute with ArcS and each other. QueF-like (QueF-L), is a homologue of the bacterial enzyme QueF, which catalyzes the NADPH-dependent reduction of preQ0 to 7-aminomethyl-7-deazaguanine (preQ1) in the queuosine pathway Pyrobaculum calidifontis
metabolism in the Euryarchaeota, the last step of the archaeosine biosynthetic pathway involves the amidation of a nitrile group on an archaeosine precursor to give formamidine, a reaction catalyzed by the enzyme archaeosine synthase (ArcS). Most Crenarchaeota lack ArcS, but possess two proteins that inversely distribute with ArcS and each other, and are implicated in G+ biosynthesis. One of these is the protein QueF-like (QueF-L) from Pyrobaculum calidifontis, which demonstrates the catalytic activity of QueF-L. Possible routes to G+-tRNA in Crenarchaeota possessing QueF-like (QueF-L) enzymes compared to the known pathway in Euryarchaeota that utilizes ArcS to carry out the amidation of preQ0-modified tRNA, overview Pyrobaculum calidifontis
additional information the conservation of Cys21 in QueF-L (Pyrobaculum calidifontis QueF-L numbering) and QueF (Cys55 inBacillus subtilis QueF numbering, PDB ID 4F8B), which in QueF participates in the catalytic mechanism via nucleophilic attack of the thiol group on the nitrile of preQ0 to form a covalent thioimide intermediate, suggests that QueF-L might utilize a similar intermediate in the mechanism to form the formamidine of G+ Pyrobaculum calidifontis
physiological function enzyme QueF-L functions as an amidinotransferase in the biosynthesis of G+-modified tRNA Pyrobaculum calidifontis