Document Detail


Molecular and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329.
MedLine Citation:
PMID:  21498645     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Biodegradation pathways of synthetic nitroaromatic compounds and anilines are well documented, but little is known about those of nitroanilines. We previously reported that the initial step in 5-nitroanthranilic acid (5NAA) degradation by Bradyrhizobium sp. strain JS329 is a hydrolytic deamination to form 5-nitrosalicylic acid (5NSA), followed by ring fission catalyzed by 5NSA dioxygenase. The mechanism of release of the nitro group was unknown. In this study, we subcloned, sequenced, and expressed the genes encoding 5NAA deaminase (5NAA aminohydrolase, NaaA), 5NSA dioxygenase (NaaB) and lactonase (NaaC), the key genes responsible for 5NAA degradation. Sequence analysis and enzyme characterization revealed that NaaA is a hydrolytic metalloenzyme with a narrow substrate range. The nitro group is spontaneously eliminated as nitrite concomitant with the formation of a lactone from the ring fission product of 5NSA dioxygenation. The elimination of the nitro group during lactone formation is a previously unreported mechanism for denitration of nitro aliphatic compounds.
Authors:
Yi Qu; Jim C Spain
Related Documents :
3200915 - Suprathreshold sour taste intensity and pleasantness perception with age.
3560535 - Comparison of pancreatic exocrine secretion via endogenous secretin by intestinal infus...
12559725 - Vitrification of in vitro cultured rabbit morulae.
25379995 - Synthesis and cytotoxicity of triterpenoids derived from betulin and betulinic acid via...
3395325 - Activation of protein kinase c by cis- and trans-fatty acids and its potentiation by di...
3019415 - Elongation of c20 polyunsaturated fatty acids by human skin fibroblasts.
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2011-04-15
Journal Detail:
Title:  Journal of bacteriology     Volume:  193     ISSN:  1098-5530     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2011 Jun 
Date Detail:
Created Date:  2011-05-27     Completed Date:  2011-08-04     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3057-63     Citation Subset:  IM    
Affiliation:
School of Civil and Environmental Engineering, Georgia Institute of Technology, Atlanta, GA 30332-0512, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/GU188569
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Aminohydrolases / genetics,  metabolism
Bacterial Proteins / genetics,  metabolism*
Biodegradation, Environmental*
Bradyrhizobium / metabolism*
Cloning, Molecular
Environmental Pollutants / metabolism
Gene Expression Regulation, Bacterial / physiology
Molecular Sequence Data
Molecular Structure
ortho-Aminobenzoates / chemistry,  metabolism*
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Environmental Pollutants; 0/ortho-Aminobenzoates; EC 3.5.4.-/Aminohydrolases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The Paf1 complex represses ARG1 transcription in Saccharomyces cerevisiae by promoting histone modif...
Next Document:  Cloning of the major outer membrane protein expression locus in Anaplasma platys and seroreactivity ...