Psychrophilic enzymes: a thermodynamic challenge

Gerday, Charles; Aittaleb, Mohamed; Arpigny, Jean Louis; Baise, Etienne; Chessa, Jean-Pierre; Garsoux, Geneviève; Petrescu, Ioan; Feller, Georges

doi:10.1016/s0167-4838(97)00093-9

Cited by 275 publications

(173 citation statements)

References 44 publications

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“…As expected, the half-life of activity of the wild-type and the native recombinant PGK are similar. Furthermore, both enzymes exhibit a very reduced thermostability, giving evidence of their psychrophilic character (31). Surprisingly, the thermostability of the His-tagged recombinant PGK was significantly increased, although remaining lower than that of the mesophilic enzyme.…”

Section: Resultsmentioning

confidence: 99%

Structural, Kinetic, and Calorimetric Characterization of the Cold-active Phosphoglycerate Kinase from the AntarcticPseudomonas sp. TACII18

Bentahir

Feller

Aittaleb

et al. 2000

Journal of Biological Chemistry

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The gene encoding the phosphoglycerate kinase (PGK) from the Antarctic Pseudomonas sp. TACII18 has been cloned and found to be inserted between the genes encoding for glyceraldhyde-3-phosphate dehydrogenase and fructose aldolase. The His-tagged and the native recombinant PGK from the psychrophilic Pseudomonas were expressed in Escherichia coli. The wild-type and the native recombinant enzymes displayed identical properties, such as a decreased thermostability and a 2-fold higher catalytic efficiency at 25°C when compared with the mesophilic PGK from yeast. These properties, which reflect typical features of cold-adapted enzymes, were strongly altered in the His-tagged recombinant PGK. The structural model of the psychrophilic PGK indicated that a key determinant of its low stability is the reduced number of salt bridges, surface charges, and aromatic interactions when compared with mesophilic and thermophilic PGK. Differential scanning calorimetry of the psychrophilic PGK revealed unusual variations in its conformational stability for the free and substrate-bound forms. In the free form, a heatlabile and a thermostable domain unfold independently. It is proposed that the heat-labile domain acts as a destabilizing domain, providing the required flexibility around the active site for catalysis at low temperatures.

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Section: Resultsmentioning

confidence: 99%

Structural, Kinetic, and Calorimetric Characterization of the Cold-active Phosphoglycerate Kinase from the AntarcticPseudomonas sp. TACII18

Bentahir

Feller

Aittaleb

et al. 2000

Journal of Biological Chemistry

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“…The correlation between the molecular structure and cold adaption of CLPs is elucidated by comparing with mesophilic and thermophilic lipases using site-directed mutagenesis and crystal studies (Narinx et al 1997;Wintrode et al 2000). The molecular structure of lipase from Pseudomonas immobilis and Pseudomonas fragi IFO 3458 when compared with their mesophilic counterpart revealed the features for cold adaption Alquati et al 2002), which are very low content of arginine residues in comparison to lysine residues, low content of proline residues, weak hydrophobic core, very less number of salt bridges and very less number of aromatic-aromatic interactions Gerday et al 1997).…”

Section: Structural Features and Cold Adaptionmentioning

confidence: 99%

Cold active lipases – an update

Kavitha

2016

Frontiers in Life Science

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Cold active lipases (CLPs) are gaining importance nowadays as they are increasingly used in fine chemical synthesis, bioremediation, food processing and as detergent additive. These enzymes exhibit high catalytic activity at low temperatures and flexibility to act at low water medium. Since they are active at low temperatures consume less energy and also stabilize fragile compounds in the reaction medium. CLPs are commonly obtained from psychrophilic microorganisms which thrive in cold habitats. Compared to mesophilic and thermophilic lipases, only a few CLPs were studied and industrially exploited so far. CLPs (C. antarctica lipase-A and C. antarctica lipase-B) from Candida antarctica isolated from Antarctic region are the well studied and industrially employed, and many are being followed up. This review updates the CLPs reported recently and the industrial applications of CLPs. ARTICLE HISTORY

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“…Several reviews summarized the properties of proteins isolated from thermophiles (Jaenicke and Zavodsky, 1990;Jaenicke, 1991;Adams, 1993;Vieille et al, 1996;Jaenicke and Böhm, 1998;Niehaus et al, 1999;Vieille and Zeikus, 2001;Sterner and Liebl, 2001) and psychrophiles Gerday et al 1997;Sanders et al, 2003;Georlette et al 2004;Siddiqui and Cavicchioli, 2006). Comprehensive studies on crystal structures of thermophilic proteins did not reveal unusual conformations specific to the source type (Petukhov et A c c e p t e d m a n u s c r i p t 5 al., 1997; Facchiano et al, 1998;Karshikoff and Ladenstein, 1998;Szilagyi and Zavodszky, 2000;Kumar et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…In order to understand the structural requirements for protein adaptation to heat or cold, the amino acid composition of proteins isolated from (hyper)thermophiles (Jaenicke, 1991;Jaenicke and Böhm, 1998;Vieille and Zeikus, 2001;Sterner and Liebl, 2001) or psychrophiles Gerday et al 1997;Sanders et al, 2003) has long been compared with that of mesophiles. Some of these investigations have been focused on the whole genome of extremophilic microorganisms, thus considering the total protein content of the selected microbial sources.…”

Section: Introductionmentioning

confidence: 99%

Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition

Vendittis

Castellano

Cotugno

et al. 2008

Journal of Theoretical Biology

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting galley proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A c c e p t e d m a n u s c r i p t A c c e p t e d m a n u s c r i p t 2 AbstractThe growth temperature adaptation of six model proteins has been studied in

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Psychrophilic enzymes: a thermodynamic challenge

Cited by 275 publications

References 44 publications

Structural, Kinetic, and Calorimetric Characterization of the Cold-active Phosphoglycerate Kinase from the AntarcticPseudomonas sp. TACII18

Structural, Kinetic, and Calorimetric Characterization of the Cold-active Phosphoglycerate Kinase from the AntarcticPseudomonas sp. TACII18

Cold active lipases – an update

Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition

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