RT Journal Article SR Electronic(1) A1 Liu, Xueqian A1 Dong, Yangpeng A1 Li, Xiaomin A1 Ren, Yi A1 Li, Yanxia A1 Wang, Wei A1 Wang, Lei A1 Feng, LuYR 2010 T1 Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2 JF Microbiology, VO 156 IS 2 SP 589 OP 595 DO https://doi.org/10.1099/mic.0.031880-0 PB Microbiology Society, SN 1465-2080, AB Anthranilate is an important intermediate of tryptophan metabolism. In this study, a hydroxylase system consisting of an FADH2-utilizing monooxygenase (GTNG_3160) and an FAD reductase (GTNG_3158), as well as a bifunctional riboflavin kinase/FMN adenylyltransferase (GTNG_3159), encoded in the anthranilate degradation gene cluster in Geobacillus thermodenitrificans NG80-2 were functionally characterized in vitro. GTNG_3159 produces FAD to be reduced by GTNG_3158 and the reduced FAD (FADH2) is utilized by GTNG_3160 to convert anthranilate to 3-hydroxyanthranilate (3-HAA), which is further degraded to acetyl-CoA through a meta-cleavage pathway also encoded in the gene cluster. Utilization of this pathway for the degradation of anthranilate and tryptophan by NG80-2 under physiological conditions was confirmed by real-time RT-PCR analysis of representative genes. This is believed to be the first time that the degradation pathway of anthranilate via 3-HAA has been characterized in a bacterium. This pathway is likely to play an important role in the survival of G. thermodenitrificans in the oil reservoir conditions from which strain NG80-2 was isolated., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.031880-0