Additional role of nicotinic acid hydroxylase for the transformation of 3-succinoyl-pyridine by Pseudomonas sp. JY-Q
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Authors
Li, Jun
Li, Shanshan
Xie, Linlin
Chen, Guoqing
Shen, Mingjie
Pan, Fanda
Shu, Ming
Yang, Yang
Jiao, Yang
Zhang, Fuming
Issue Date
2021-03-01
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
Abstract
Nicotine and nicotinic acid (NA) are both considered to be representatives of N-heterocyclic aromatic compounds, and their degradation pathways have been revealed in Pseudomonas species. However, the cooccurrence of these two pathways has only been observed in Pseudomonas sp. strain JY-Q. The nicotine pyrrolidine catabolism pathway of strain JY-Q consists of the functional modules Nic1, Spm, and Nic2. The module enzyme, 3-succinoylpyridine monooxygenase (Spm), catalyzes transformation of 3-succinoyl-pyridine (SP) to 6-hydroxy-3-succinoyl-pyridine (HSP). There exist two homologous but not identical Spm enzymes (namely, Spm1 and Spm2) in JY-Q. However, when spm1 and spm2 were both in-frame deleted, the mutant still grew well in basic salt medium (BSM) supplemented with nicotine as the sole carbon/nitrogen nutrition, suggesting that there exists an alternative pathway responsible for SP catabolism in JY-Q. NicAB, an enzyme accounting for NA hydroxylation, contains reorganized domains similar to those of Spm. When the JY-Q_nicAB gene (nicAB in strain JY-Q) was introduced into another Pseudomonas strain, one that is unable to degrade NA, the resultant recombinant strain exhibited the ability to transform SP to HSP, but without the ability to metabolize NA. Here, we conclude that NicAB in strain JY-Q exhibits an additional role in SP transformation. The other genes in the NA cluster, NicXDFE (Nic2 homolog), then also exhibit a role in subsequent HSP metabolism for energy yield. This finding also suggests that the cooccurrence of nicotine and NA degradation genes in strain JY-Q represents an advantage for JY-Q, making it more effective and flexible for the degradation of nicotine.
Description
Applied Environmental Microbiology, 87, e02740-20
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Full Citation
Additional role of nicotinic acid hydroxylase for the transformation of 3-succinoyl-pyridine by Pseudomonas sp. JY-Q. J. Li, S. Li, L. Xie, G. Chen, M. Shen, F. Pan, M. Shu, Y. Yang, Y. Jiao, F. Zhang, R. J. Linhardt, W. Zhong, Applied Environmental Microbiology, 87, e02740-20, 2021.
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Journal
Volume
Issue
PubMed ID
DOI
ISSN
10985336
992240
992240