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PMID:22657530

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Citation

Selvin, J, Kennedy, J, Lejon, DP, Kiran, GS and Dobson, AD (2012) Isolation identification and biochemical characterization of a novel halo-tolerant lipase from the metagenome of the marine sponge Haliclona simulans. Microb. Cell Fact. 11:72

Abstract

Lipases (EC 3.1.1.3) catalyze the hydrolysis of triacyl glycerol to glycerol and are involved in the synthesis of both short chain and long chain acylglycerols. They are widely used industrially in various applications, such as baking, laundry detergents and as biocatalysts in alternative energy strategies. Marine ecosystems are known to represent a large reservoir of biodiversity with respect to industrially useful enzymes. However the vast majority of microorganisms within these ecosystems are not readily culturable. Functional metagenomic based approaches provide a solution to this problem by facilitating the identification of novel enzymes such as the halo-tolerant lipase identified in this study from a marine sponge metagenome.

Links

PubMed PMC3544137 Online version:10.1186/1475-2859-11-72

Keywords

Amino Acid Sequence; Animals; Calcium/chemistry; Cloning, Molecular; Haliclona/genetics; Haliclona/metabolism; Hydrogen-Ion Concentration; Ions/chemistry; Lipase/chemistry; Lipase/classification; Lipase/genetics; Metagenome; Metals/chemistry; Molecular Sequence Data; Phylogeny; Plasmids/genetics; Plasmids/metabolism; Protein Stability; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Sequence Alignment; Sodium Chloride/chemistry; Substrate Specificity; Temperature

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

9BACT:I4AY78

GO:0016298: lipase activity

ECO:0000314:

F

Table 1 shows the relative activity of lpc53e1 on a range of substrates

complete
CACAO 10925

9BACT:I4AY78

enables

GO:0016298: lipase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

Notes

See also

References

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