Choice of microbial host for the naphthalene dioxygenase bioconversion

1996 ◽  
Vol 16 (5) ◽  
pp. 274-279 ◽  
Author(s):  
D. Wilkinson ◽  
J M Ward ◽  
J M Woodley
Keyword(s):  
Naphthalene Dioxygenase ◽  
Microbial Host

scholarly journals Desaturation and oxygenation of 1,2-dihydronaphthalene by toluene and naphthalene dioxygenase.

1995 ◽  
Vol 177 (20) ◽  
pp. 5799-5805 ◽  
Author(s):  
D S Torok ◽  
S M Resnick ◽  
J M Brand ◽  
D L Cruden ◽  
D T Gibson
Keyword(s):  
Naphthalene Dioxygenase

scholarly journals Microbially guided discovery and biosynthesis of biologically active natural products

2021 ◽  
Author(s):  
Ankur Sarkar ◽  
Edward Kim ◽  
Taehwan Jang ◽  
Akarawin Hongdusit ◽  
Hyungjun Kim ◽  
...  
Keyword(s):  
Natural Products ◽  
Tyrosine Phosphatase ◽  
Biologically Active ◽  
Allosteric Site ◽  
Terpene Synthases ◽  
Guided Discovery ◽  
Detection Systems ◽  
Treatment Of Diabetes ◽  
Active Natural ◽  
Microbial Host

Abstract The design of small molecules that inhibit disease-relevant proteins represents a longstanding challenge of medicinal chemistry. Here, we describe an approach for encoding this challenge—the inhibition of a human drug target—into a microbial host and using it to guide the discovery and biosynthesis of targeted, biologically active natural products. This approach identified two previously unknown terpenoid inhibitors of protein tyrosine phosphatase 1B (PTP1B), an elusive therapeutic target for the treatment of diabetes and cancer. Both inhibitors appear to target an allosteric site, which confers selectivity, and can inhibit PTP1B in living cells. A screen of 24 uncharacterized terpene synthases from a pool of 4,464 genes uncovered additional hits, demonstrating a scalable discovery approach, and the incorporation of different PTPs into the microbial host yielded alternative PTP-specific detection systems. Findings illustrate the potential for using microbes to discover and build natural products that exhibit precisely defined biochemical activities yet possess unanticipated structures and/or binding sites.

scholarly journals A Recently Assembled Degradation Pathway for 2,3-Dichloronitrobenzene in Diaphorobacter sp. Strain JS3051

mBio ◽  
2021 ◽  
Author(s):  
Tao Li ◽  
Yi-Zhou Gao ◽  
Jia Xu ◽  
Shu-Ting Zhang ◽  
Yuan Guo ◽  
...  
Keyword(s):  
Common Ancestor ◽  
Degradation Pathway ◽  
Nitroaromatic Compounds ◽  
Naphthalene Dioxygenase ◽  
Evolutionary Mechanisms ◽  
Catabolic Pathways

Because anthropogenic nitroaromatic compounds have entered the biosphere relatively recently, exploration of the recently evolved catabolic pathways can provide clues for adaptive evolutionary mechanisms in bacteria. The concept that nitroarene dioxygenases shared a common ancestor with naphthalene dioxygenase is well established.

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