Cloned (Comment) | Organism |
---|---|
gene queF-L, recombinant overexpression of His6-tagged enzyme in Escherichia coli | Pyrobaculum calidifontis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Pyrobaculum calidifontis | A3MSP1 | - |
- |
Pyrobaculum calidifontis JCM 11548 | A3MSP1 | - |
- |
Pyrobaculum calidifontis VA1 | A3MSP1 | - |
- |
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 | 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 | 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 | 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 |