PreQ1 synthase

PreQ1 synthase
Identifiers
EC no.1.7.1.13
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
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NCBIproteins

PreQ1 synthase (EC 1.7.1.13) is an enzyme that catalyzes the chemical reaction

2D representation of the chemical structure of Q27094033.
7-cyano-7-deazaguanine
+ 2 NADPH
 
 
2 H+
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left and minor reverse product(s) to bottom left
2 H+
 
 
2D representation of the chemical structure of Q27120591.
7-aminomethyl-7-deazaguanine
+ 2 NADP+
 

The substrates of this enzyme are 7-cyano-7-deazaguanine, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and two protons. Its products are 7-aminomethyl-7-deazaguanine and oxidised NADP+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase. Other names in common use include YkvM, QueF, preQ0 reductase, preQ0 oxidoreductase, 7-cyano-7-deazaguanine reductase, 7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase, queuine synthase and queuine:NADP+ oxidoreductase: (the last two are misleading as queuine is not the product). The enzyme is part of the biosynthetic pathway to modified nucleoside, queuosine. As of 2012, this was the only enzyme known to directly catalyze the reduction of a nitrile group to a primary amine.

References

  1. ↑ Enzyme 1.7.1.13 at KEGG Pathway Database.
  2. ↑ Iwata-Reuyl D; Reader, JS; Swairjo, MA; De Crécy-Lagard, V; Lee, B; Iwata-Reuyl, D (2005). "From cyclohydrolase to oxidoreductase: Discovery of nitrile reductase activity in a common fold". Proc. Natl. Acad. Sci. U.S.A. 102 (12): 4264–9. Bibcode:2005PNAS..102.4264V. doi:10.1073/pnas.0408056102. PMC 555470. PMID 15767583.
  3. ↑ Yokoyama S, Miyazawa T, Iitaka Y, Yamaizumi Z, Kasai H, Nishimura S (1979). "Three-dimensional structure of hyper-modified nucleoside Q located in the wobbling position of tRNA". Nature. 282 (5734): 107–9. Bibcode:1979Natur.282..107Y. doi:10.1038/282107a0. PMID 388227. S2CID 4313325.
  4. ↑ Kuchino Y, Kasai H, Nihei K, Nishimura S (1976). "Biosynthesis of the modified nucleoside Q in transfer RNA". Nucleic Acids Res. 3 (2): 393–8. doi:10.1093/nar/3.2.393. PMC 342909. PMID 1257053.
  5. ↑ JA; Noguchi, S; Nishimura, S; Ohgi, T; Goto, T; Crain, PF; McCloskey, JA (1978). "Structure determination of a nucleoside Q precursor isolated from E. coli tRNA: 7-(aminomethyl)-7-deazaguanosine". Nucleic Acids Res. 5 (7): 2289–96. doi:10.1093/nar/5.7.2289. PMC 342163. PMID 353740.
  6. ↑ Nishimura S; Yamaizumi, Z; Ohgi, T; Goto, T; Nishimura, Y; Hirota, Y; Nishimura, S (1978). "Isolation of Q nucleoside precursor present in tRNA of an E. coli mutant and its characterization as 7-(cyano)-7-deazaguanosine". Nucleic Acids Res. 5 (11): 4215–23. doi:10.1093/nar/5.11.4215. PMC 342744. PMID 364423.
  7. ↑ Swairjo M.A.; Reddy R.R.; Lee B.; Van Lanen S.G.; Brown S.; de Crécy-Lagard V.; Iwata-Reuyl D, Schimmel P; preliminary X-ray characterization of the nitrile reductase QueF: a queuosine-biosynthesis enzyme (2005). "Crystallization". Acta Crystallogr. F. 61 (Pt 10): 945–8. doi:10.1107/S1744309105029246. PMC 1991305. PMID 16511203.
  8. ↑ Chikwana, V.M.; Stec, B.; Lee, B.W.K.; de Crécy-Lagard, V.; Iwata-Reuyl, D.; Swairjo, M.A. (2012). "Structural basis of biological nitrile reduction". Journal of Biological Chemistry. 287 (36): 30560–70. doi:10.1074/jbc.m112.388538. PMC 3436371. PMID 22787148.