PreQ1 synthase
This article will address the topic of PreQ1 synthase, which has currently generated great interest and debate. PreQ1 synthase is a relevant topic in today's society, since it impacts various areas of daily life. Throughout history, PreQ1 synthase has been the subject of analysis and reflection, raising conflicting opinions and provoking a wide variety of reactions. In this sense, it is crucial to thoroughly analyze PreQ1 synthase to understand its impact on society and explore possible solutions or approaches to address this issue. In order to provide a comprehensive and enriching vision, this article will compile various perspectives and arguments related to PreQ1 synthase, with the purpose of offering a global and reflective look at this issue.
| 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 | ||||||||
| |||||||||
In enzymology, a preQ1 synthase (EC 1.7.1.13) is an enzyme that catalyzes the chemical reaction
- 7-aminomethyl-7-carbaguanine + 2 NADP+ 7-cyano-7-carbaguanine + 2 NADPH + 2 H+
Thus, the two substrates of this enzyme are 7-aminomethyl-7-carbaguanine and NADP+, whereas its 3 products are 7-cyano-7-carbaguanine, NADPH, and H+.
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 (incorrect as queuine is not the product), and queuine:NADP+ oxidoreductase (incorrect as queuine is not the product).
References
- 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.
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