Literature DB >> 16086253

The putative lipase, AF1763, from Archaeoglobus fulgidusis is a carboxylesterase with a very high pH optimum.

Monika Rusnak1, Jens Nieveler, Rolf D Schmid, Ralf Petri.   

Abstract

The open reading frame AF1763, annotated as a putative lipase gene (lipA) of the hyperthermophilic archaeon, Archaeoglobus fulgidus DSM 4304, was cloned and over-expressed in E. coli. A sequence analysis of LipA and the investigation of a truncated enzyme implied a special function of the C-terminal part of LipA. The substrate spectrum of the enzyme suggested that LipA is a carboxylesterase rather than a canonical lipase. The enzyme showed optimal activity at 70 degrees C and between pH 10 and 11, which is among the most alkaline pH range detected for hydrolases.

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Year:  2005        PMID: 16086253     DOI: 10.1007/s10529-005-5621-1

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN: 0141-5492            Impact factor:   2.461


  3 in total

1.  N-terminal domain replacement changes an archaeal monoacylglycerol lipase into a triacylglycerol lipase.

Authors:  Surabhi Soni; Sneha S Sathe; Rutuja R Sheth; Prince Tiwari; Rajesh-Kumar N Vadgama; Annamma Anil Odaneth; Arvind M Lali; Sanjeev K Chandrayan
Journal:  Biotechnol Biofuels       Date:  2019-05-06       Impact factor: 6.040

2.  Comparative molecular docking and molecular-dynamic simulation of wild-type- and mutant carboxylesterase with BTA-hydrolase for enhanced binding to plastic.

Authors:  Fatana Lameh; Abdul Qadeer Baseer; Abubakar Garba Ashiru
Journal:  Eng Life Sci       Date:  2021-11-15       Impact factor: 2.678

Review 3.  Carboxylic ester hydrolases from hyperthermophiles.

Authors:  Mark Levisson; John van der Oost; Servé W M Kengen
Journal:  Extremophiles       Date:  2009-06-21       Impact factor: 2.395

  3 in total

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