Extremely stable indole-3-glycerol-phosphate synthase from hyperthermophilic archaeon Pyrococcus furiosus.


Journal

Extremophiles : life under extreme conditions
ISSN: 1433-4909
Titre abrégé: Extremophiles
Pays: Germany
ID NLM: 9706854

Informations de publication

Date de publication:
Jan 2019
Historique:
received: 21 05 2018
accepted: 24 09 2018
pubmed: 29 9 2018
medline: 2 5 2019
entrez: 29 9 2018
Statut: ppublish

Résumé

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 V

Identifiants

pubmed: 30264228
doi: 10.1007/s00792-018-1061-4
pii: 10.1007/s00792-018-1061-4
doi:

Substances chimiques

Archaeal Proteins 0
Indole-3-Glycerol-Phosphate Synthase EC 4.1.1.48

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

69-77

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Auteurs

Muhammad Arif (M)

School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore, 54590, Pakistan.

Naeem Rashid (N)

School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore, 54590, Pakistan. naeem.ff.sbs@pu.edu.pk.

Sumera Perveen (S)

School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore, 54590, Pakistan.

Qamar Bashir (Q)

School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore, 54590, Pakistan.

Muhammad Akhtar (M)

School of Biological Sciences, University of Southampton, Southampton, SO16 7PX, UK.

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Classifications MeSH