Activity Enhancement Based on the Chemical Equilibrium of Multiple-Subunit Nitrile Hydratase from Bordetella petrii View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-09

AUTHORS

Yi Liu, Ping Liu, Lu Lin, Yueqin Zhao, Wenjuan Zhong, Lunjie Wu, Zhemin Zhou, Weifeng Sun

ABSTRACT

The maturation mechanism of nitrile hydratase (NHase) of Pseudomonas putida NRRL-18668 was discovered and named as "self-subunit swapping." Since the NHase of Bordetella petrii DSM 12804 is similar to that of P. putida, the NHase maturation of B. petrii is proposed to be the same as that of P. putida. However, there is no further information on the application of NHase according to these findings. We successfully rapidly purified NHase and its activator through affinity his tag, and found that the cell extracts of NHase possessed multiple types of protein ingredients including α, β, α2β2, and α(P14K)2 who were in a state of chemical equilibrium. Furthermore, the activity was significantly enhanced through adding extra α(P14K)2 to the cell extracts of NHase according to the chemical equilibrium. Our findings are useful for the activity enhancement of multiple-subunit enzyme and for the first time significantly increased the NHase activity according to the chemical equilibrium. More... »

PAGES

3-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12010-016-2079-7

DOI

http://dx.doi.org/10.1007/s12010-016-2079-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016383813

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27075457


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