Vaitekūnas Justas, Gasparavičiūtė Renata, Rutkienė Rasa, Tauraitė Daiva, Meškys Rolandas
Department of Molecular Microbiology and Biotechnology, Institute of Biochemistry, Vilnius University, Vilnius, Lithuania
Department of Molecular Microbiology and Biotechnology, Institute of Biochemistry, Vilnius University, Vilnius, Lithuania.
Appl Environ Microbiol. 2015 Dec 11;82(4):1264-1273. doi: 10.1128/AEM.02975-15. Print 2016 Feb 15.
Rhodococcus rhodochrous PY11 (DSM 101666) is able to use 2-hydroxypyridine as a sole source of carbon and energy. By investigating a gene cluster (hpo) from this bacterium, we were able to reconstruct the catabolic pathway of 2-hydroxypyridine degradation. Here, we report that in Rhodococcus rhodochrous PY11, the initial hydroxylation of 2-hydroxypyridine is catalyzed by a four-component dioxygenase (HpoBCDF). A product of the dioxygenase reaction (3,6-dihydroxy-1,2,3,6-tetrahydropyridin-2-one) is further oxidized by HpoE to 2,3,6-trihydroxypyridine, which spontaneously forms a blue pigment. In addition, we show that the subsequent 2,3,6-trihydroxypyridine ring opening is catalyzed by the hypothetical cyclase HpoH. The final products of 2-hydroxypyridine degradation in Rhodococcus rhodochrous PY11 are ammonium ion and α-ketoglutarate.
红平红球菌PY11（DSM 101666）能够利用2-羟基吡啶作为唯一的碳源和能源。通过研究该细菌的一个基因簇（hpo），我们得以重建2-羟基吡啶的分解代谢途径。在此，我们报告在红平红球菌PY11中，2-羟基吡啶的初始羟基化反应由一种四组分双加氧酶（HpoBCDF）催化。双加氧酶反应的产物（3,6-二羟基-1,2,3,6-四氢吡啶-2-酮）被HpoE进一步氧化为2,3,6-三羟基吡啶，后者会自发形成一种蓝色色素。此外，我们表明随后的2,3,6-三羟基吡啶开环反应由假定的环化酶HpoH催化。红平红球菌PY11中2-羟基吡啶降解的最终产物是铵离子和α-酮戊二酸。
