PreQ1 synthase
| PreQ1 synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.7.1.13 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
PreQ1 synthase (EC 1.7.1.13) is an enzyme that catalyzes the chemical reaction
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+.[1][2][3]
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.[4][5][6][7] As of 2012, this was the only enzyme known to directly catalyze the reduction of a nitrile group to a primary amine.[8]
References
- ^ Enzyme 1.7.1.13 at KEGG Pathway Database.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.