In:
Applied and Environmental Microbiology, American Society for Microbiology, Vol. 69, No. 5 ( 2003-05), p. 2748-2754
Abstract:
Rhodococcus ( opacus ) erythropolis HL PM-1 grows on 2,4,6-trinitrophenol or 2,4-dinitrophenol (2,4-DNP) as a sole nitrogen source. The NADPH-dependent F 420 reductase (NDFR; encoded by npdG ) and the hydride transferase II (HTII; encoded by npdI ) of the strain were previously shown to convert both nitrophenols to their respective hydride Meisenheimer complexes. In the present study, npdG and npdI were amplified from six 2,4-DNP degrading Rhodococcus spp. The genes showed sequence similarities of 86 to 99% to the respective npd genes of strain HL PM-1. Heterologous expression of the npdG and npdI genes showed that they were involved in 2,4-DNP degradation. Sequence analyses of both the NDFRs and the HTIIs revealed conserved domains which may be involved in binding of NADPH or F 420 . Phylogenetic analyses of the NDFRs showed that they represent a new group in the family of F 420 -dependent NADPH reductases. Phylogenetic analyses of the HTIIs revealed that they form an additional group in the family of F 420 -dependent glucose-6-phosphate dehydrogenases and F 420 -dependent N 5 , N 10 -methylenetetrahydromethanopterin reductases. Thus, the NDFRs and the HTIIs may each represent a novel group of F 420 -dependent enzymes involved in catabolism.
Type of Medium:
Online Resource
ISSN:
0099-2240
,
1098-5336
DOI:
10.1128/AEM.69.5.2748-2754.2003
Language:
English
Publisher:
American Society for Microbiology
Publication Date:
2003
detail.hit.zdb_id:
223011-2
detail.hit.zdb_id:
1478346-0
SSG:
12
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