Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly-->Pro substitution near the active site on its catalytic activity and stability.

@article{Kulakova2004ColdactiveEF,
  title={Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly-->Pro substitution near the active site on its catalytic activity and stability.},
  author={L. Kulakova and A. Galkin and T. Nakayama and T. Nishino and N. Esaki},
  journal={Biochimica et biophysica acta},
  year={2004},
  volume={1696 1},
  pages={
          59-65
        }
}
The gene encoding an esterase (PsyEst) of Psychrobacter sp. Ant300, a psychrophilic bacterium isolated from Antarctic soil, was cloned, sequenced, and expressed in Escherichia coli. PsyEst, which is a member of hormone-sensitive lipase (HSL) group of the lipase/esterase family, is a cold-active, themolabile enzyme with high catalytic activity at low temperatures (5-25 degrees C), low activation energy (e.g., 4.6 kcal/mol for hydrolysis of p-nitrophenyl butyrate), and a t(1/2) value of 16 min… Expand
The hormone-sensitive lipase from Psychrobacter sp. TA144: new insight in the structural/functional characterization.
TLDR
Cold-adapted esterases and lipases have been found to be dominant activities throughout the cold marine environment, indicating their importance in bacterial degradation of the organic matter and the region surrounding PsyHSL catalytic site showed an unexpected homology with the human HSL. Expand
A novel cold-adapted esterase from Salinisphaera sp. P7-4: gene cloning, overproduction, and characterization.
Salinisphaera sp. P7-4 was isolated from the intestine of silver whiting, Sillago japonicas caught in the Pacific Ocean, and the esterase gene was cloned using the shotgun method. The amino acidExpand
Characterization of a cold-active esterase from Serratia sp. and improvement of thermostability by directed evolution
TLDR
EstS was a novel cold-active and salt-tolerant esterase and half-life of mutant 1-D5 was enhanced by 1.4 times compared with WT and the features of EstS are interesting and can be exploited for commercial applications. Expand
Biochemical characterization and structural analysis of a new cold-active and salt-tolerant esterase from the marine bacterium Thalassospira sp.
TLDR
The hypothesis is that a high methionine content, less hydrogen bonds and less ion pairs render the enzyme more flexible at low temperatures, suggesting that it could function as an interesting candidate for biotechnological applications. Expand
A cold-adapted esterase from psychrotrophic Pseudoalteromas sp. strain 643A
TLDR
A psychrotrophic bacterium producing a cold-adapted esterase upon growth at low temperatures was isolated from the alimentary tract of Antarctic krill Euphasiasuperba Dana, and analysis of the amino acid sequence of EstA suggests that it is a member of the GDSL-lipolytic enzymes family. Expand
Characterization of a cold-active lipase from Psychrobacter cryohalolentis K5T and its deletion mutants
TLDR
The results prove that the N-terminal domain of Lip1Pc has a fundamental impact on the activity and stability of the protein. Expand
Isolation and Characterization of EstC, a New Cold-Active Esterase from Streptomyces coelicolor A3(2)
TLDR
One of the recombinant enzymes, EstC, showed interesting cold-active esterase activity with a strong potential for the production of valuable esters, suggesting it could function as an interesting candidate for organic synthesis of short-chain esters such as flavors. Expand
Isolation and Characterization of EstC , a New Cold-Active Esterase from Streptomyces coelicolor A 3 ( 2 )
The genome sequence of Streptomyces coelicolor A3(2) contains more than 50 genes coding for putative lipolytic enzymes. Many studies have shown the capacity of this actinomycete to store importantExpand
A novel extracellular cold-active esterase of Pseudomonas sp. TB11 from glacier No.1: Differential induction, purification and characterisation
Abstract The production, purification, characterization and application of a novel cold active esterase by Pseudomonas sp. TB11 are described herein. A new finding regarding the production ofExpand
A novel esterase from Paenibacillus sp. PBS-2 is a new member of the β-lactamase belonging to the family VIII lipases/esterases.
TLDR
The PBS-2 generated in Escherichia coli led to the identification of a clone with lipolytic activity that has potential as a biocatalyst and detergent additive for use at low temperatures and is cold-adapted. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 30 REFERENCES
Primary Structure and Catalytic Properties of a Cold-active Esterase from a Psychrotroph, Acinetobacter sp. Strain No. 6. Isolated from Siberian Soil
TLDR
A gene coding for a cold-active esterase from a genomic library of Acinetobacter strain No. 6, a psychrotroph isolated from Siberian soil, catalyzed the hydrolysis of esters with short-chain acyl groups and had lower activation energy and lower thermostability than do mesophilic enzymes, as expected from the cold-adapted nature of this enzyme. Expand
Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily.
TLDR
The enzyme, a 34 kDa monomeric protein, was demonstrated to be a B'-type carboxylesterase (EC 3.1.1) on the basis of substrate specificity and the action of inhibitors, and supported the previous suggestion of a catalytic triad made up of Ser-His-Asp. Expand
A cold-active esterase with a substrate preference for vinyl esters from a psychrotroph, Acinetobacter sp. strain no. 6: gene cloning, purification, and characterization ☆
Abstract It has recently been shown that fatty acid vinyl esters serve as effective acylating agents for the synthesis of esters by enzymatic transesterification in high yields. To enhance theExpand
Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1.
TLDR
A gene coding for an esterase of the psychrotrophic bacterium Pseudomonas sp. Expand
A Cold-Adapted Lipase of an Alaskan Psychrotroph,Pseudomonas sp. Strain B11-1: Gene Cloning and Enzyme Purification and Characterization
TLDR
The enzyme showed a 1,3-positional specificity toward triolein and was stable between pH 6 and 9, and the optimal pH for the enzymatic hydrolysis of tributyrin was around 8.2, while the enzyme was unstable at temperatures higher than 45°C. Expand
Nucleotide sequence of the lipase gene lip2 from the antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues.
TLDR
It is suggested that only subtle changes in the primary structure of these psychrotrophic enzymes can account for their ability to catalyze lipolysis at temperatures close to 0 degrees C. Expand
Cold-active lipolytic activity of psychrotrophic Acinetobacter sp. strain no. 6.
TLDR
Strain no. 6 extracellularly produced a lipolytic enzyme that efficiently hydrolyzed triglycerides such as soybean oil during bacterial growth even at 4 degrees C, which is potentially applicable to in-situ bioremediation or bioaugumentation of fat-contaminated cold environments. Expand
An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase.
TLDR
Comparison of the amino acid sequence of this enzyme allows us to propose that Ser165, Asp262 and His292 constitute the catalytic triad of E. coli esterase, suggesting that the enzyme exists in a monomeric form. Expand
Enzymes from psychrophilic organisms
TLDR
The comparison of the 3D structures obtained either by protein modelling or by X-ray crystallography (North Atlantic trypsin) with those of their mesophilic counterparts indicates that the molecular changes tend to increase the flexibility of the structure by a weakening of the intramolecular interactions and by an increase of the interactions with the solvent. Expand
Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella sp. strain Ac10 by rational mutagenesis
Abstract A serine alkaline protease (SapSh) from a psychrophilic bacterium Shewanella sp. strain Ac10 is a cold-active subtilase with low thermostability [Appl. Environ. Microbiol. 65 (1999)Expand
...
1
2
3
...