Extremely stable indole-3-glycerol-phosphate synthase from hyperthermophilic archaeon Pyrococcus furiosus View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2019-01

AUTHORS

Muhammad Arif, Naeem Rashid, Sumera Perveen, Qamar Bashir, Muhammad Akhtar

ABSTRACT

The gene-encoding Indole-3-glycerol phosphate synthase, a key enzyme involved in the cyclization of 1-(o-carboxyphenylamino)-1-deoxyribulose 5-phosphate, from Pyrococcus furiosus was cloned and expressed in Escherichia coli. The gene product was produced in the soluble and active form. The recombinant protein, purified to apparent homogeneity, displayed highest activity at 100 °C and pH of 5.5. The recombinant enzyme followed Michaelis-Menten kinetics exhibiting apparent Vmax and Km values of 20 ± 0.5 μmol min-1 mg-1 and 140 ± 10 µM, respectively. The activation energy, determined from the linear Arrhenius plot, was 17 ± 0.5 kJ mol-1. A unique property of PfInGPS is its stability against denaturants and temperature. There was no significant change in activity even in the presence of 8 M urea or 5 M guanidine hydrochloride. Furthermore, recombinant PfInGPS was highly thermostable with a half-life of 200 min at 100 °C. To the best of our knowledge, this is the most stable indole-3-glycerol phosphate synthase characterized to date. More... »

PAGES

1-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00792-018-1061-4

DOI

http://dx.doi.org/10.1007/s00792-018-1061-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1107273174

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30264228


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