Harthern-Flint Sarah L, Dolfing Jan, Mrozik Wojciech, Meynet Paola, Eland Lucy E, Sim Martin, Davenport Russell J
School of Engineering, Newcastle University, Newcastle upon Tyne, United Kingdom.
Faculty Engineering and Environment, Northumbria University, Newcastle upon Tyne, United Kingdom.
Front Microbiol. 2021 Jul 1;12:670928. doi: 10.3389/fmicb.2021.670928. eCollection 2021.
ATCC13557 was selected as a model organism to study oestrogen degradation based on its previous ability to degrade 17α-ethinylestradiol (EE2). Biodegradation experiments revealed that ATCC13557 was unable to metabolise EE2. However, it was able to metabolise E2 with the major metabolite being E1 with no further degradation of E1. However, the conversion of E2 into E1 was incomplete, with 11.2 and 50.6% of E2 degraded in mixed (E1-E2-EE2) and E2-only conditions, respectively. Therefore, the metabolic pathway of E2 degradation by ATCC13557 may have two possible pathways. The genome of ATCC13557 was sequenced, assembled, and mapped for the first time. The genome analysis allowed the identification of genes possibly responsible for the observed biodegradation characteristics of ATCC13557. Several genes within ATCC13557 are similar, but not identical in sequence, to those identified within the genomes of other oestrogen degrading bacteria, including strain SJTE-1 and strain KC8. Homologous gene sequences coding for enzymes potentially involved in oestrogen degradation, most commonly a cytochrome P450 monooxygenase (), extradiol dioxygenase (), and 17β-hydroxysteroid dehydrogenase (), were identified within the genome of ATCC13557. These searches also revealed a gene cluster potentially coding for enzymes involved in steroid/oestrogen degradation; 3-carboxyethylcatechol 2,3-dioxygenase, 2-hydroxymuconic semialdehyde hydrolase, 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase, 3-(3-hydroxy-phenyl)propionate hydroxylase, cytochrome P450 monooxygenase, and 3-oxosteroid 1-dehydrogenase. Further, the searches revealed steroid hormone metabolism gene clusters from the 9, 10- pathway, therefore ATCC13557 also has the potential to metabolise other steroid hormones such as cholesterol.
基于ATCC13557先前具有降解17α-乙炔雌二醇(EE2)的能力,它被选作研究雌激素降解的模式生物。生物降解实验表明,ATCC13557无法代谢EE2。然而,它能够代谢E2,主要代谢产物为E1,且E1不再进一步降解。不过,E2向E1的转化并不完全,在混合(E1-E2-EE2)和仅含E2的条件下,分别有11.2%和50.6%的E2被降解。因此,ATCC13557降解E2的代谢途径可能有两种。首次对ATCC13557的基因组进行了测序、组装和定位。基因组分析有助于识别可能导致ATCC13557呈现出所观察到的生物降解特性的基因。ATCC13557中的几个基因在序列上与其他雌激素降解细菌(包括SJTE-1菌株和KC8菌株)基因组中鉴定出的基因相似但并不相同。在ATCC13557的基因组中鉴定出了可能参与雌激素降解的同源基因序列,这些序列编码的酶最常见的有细胞色素P450单加氧酶、间二醇双加氧酶和17β-羟基类固醇脱氢酶。这些搜索还揭示了一个可能编码参与类固醇/雌激素降解的酶的基因簇;3-羧乙基儿茶酚2,3-双加氧酶、2-羟基粘康酸半醛水解酶、3-α-(或20-β)-羟基类固醇脱氢酶、3-(3-羟基苯基)丙酸羟化酶、细胞色素P450单加氧酶和3-氧代类固醇1-脱氢酶。此外,搜索还揭示了来自9,10-途径的类固醇激素代谢基因簇,因此ATCC13557也有代谢其他类固醇激素(如胆固醇)的潜力。