Literature DB >> 12785714

Molecular adaptations to cold in psychrophilic enzymes.

G Feller1.   

Abstract

Psychrophiles or cold-loving organisms successfully colonize cold environments of the Earth's biosphere. To cope with the reduction of chemical reaction rates induced by low temperatures, these organisms synthesize enzymes characterized by a high catalytic activity at low temperatures associated, however, with low thermal stability. Thanks to recent advances provided by X-ray crystallography, protein engineering and biophysical studies, we are beginning to understand the molecular adaptations responsible for these properties which appear to be relatively diverse. The emerging picture suggests that psychrophilic enzymes utilize an improved flexibility of the structures involved in the catalytic cycle, whereas other protein regions if not implicated in catalysis may or may not be subjected to genetic drift.

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Year:  2003        PMID: 12785714     DOI: 10.1007/s00018-003-2155-3

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  47 in total

1.  Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis.

Authors:  Geneviève Garsoux; Josette Lamotte; Charles Gerday; Georges Feller
Journal:  Biochem J       Date:  2004-12-01       Impact factor: 3.857

2.  Site-directed mutagenesis of a family 42 β-galactosidase from an antarctic bacterium.

Authors:  Matthew V Shumway; Peter P Sheridan
Journal:  Int J Biochem Mol Biol       Date:  2012-05-18

Review 3.  Atlantic cod trypsins: from basic research to practical applications.

Authors:  Agústa Gudmundsdóttir; Helga Margrét Pálsdóttir
Journal:  Mar Biotechnol (NY)       Date:  2005-02-17       Impact factor: 3.619

4.  Characteristics of the amylase of Arthrobacter psychrolactophilus.

Authors:  Michael R Smith; James C Zahnley
Journal:  J Ind Microbiol Biotechnol       Date:  2005-10-15       Impact factor: 3.346

5.  The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase.

Authors:  Khawar S Siddiqui; Georges Feller; Salvino D'Amico; Charles Gerday; Laura Giaquinto; Ricardo Cavicchioli
Journal:  J Bacteriol       Date:  2005-09       Impact factor: 3.490

6.  Comparative genomics of DNA fragments from six Antarctic marine planktonic bacteria.

Authors:  Joseph J Grzymski; Brandon J Carter; Edward F DeLong; Robert A Feldman; Amir Ghadiri; Alison E Murray
Journal:  Appl Environ Microbiol       Date:  2006-02       Impact factor: 4.792

7.  Crystallization and preliminary X-ray diffraction studies of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.

Authors:  Yannis Papanikolau; Iason Tsigos; Maria Papadovasilaki; Vassilis Bouriotis; Kyriacos Petratos
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2005-02-01

8.  Thirty-degree shift in optimum temperature of a thermophilic lipase by a single-point mutation: effect of serine to threonine mutation on structural flexibility.

Authors:  Monika Sharma; Rakesh Kumar; Ranvir Singh; Jagdeep Kaur
Journal:  Mol Cell Biochem       Date:  2017-02-11       Impact factor: 3.396

Review 9.  New extremophilic lipases and esterases from metagenomics.

Authors:  Olalla López-López; Maria E Cerdán; Maria I González Siso
Journal:  Curr Protein Pept Sci       Date:  2014       Impact factor: 3.272

10.  Role of disulfide bridges in the activity and stability of a cold-active alpha-amylase.

Authors:  Khawar Sohail Siddiqui; Anne Poljak; Michael Guilhaus; Georges Feller; Salvino D'Amico; Charles Gerday; Ricardo Cavicchioli
Journal:  J Bacteriol       Date:  2005-09       Impact factor: 3.490

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