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Literature summary extracted from

  • Ngo, T.D.; Ryu, B.H.; Ju, H.; Jang, E.; Park, K.; Kim, K.K.; Kim, T.D.
    Structural and functional analyses of a bacterial homologue of hormone-sensitive lipase from a metagenomic library (2013), Acta Crystallogr. Sect. D, 69, 1726-1737.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.79 drug development the requirement of dimerization for the function and stability of HSL-family enzymes focuses attention on the dimeric interface as a potential target for structure-aided drug design uncultured bacterium
3.1.1.79 synthesis the glutaraldehyde-medited crosslinked enzyme, showing increased stability, can be used as a biocatalyst in biotransformation processes uncultured bacterium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.79 gene Est25, phylogenetic analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain XL1-Blue uncultured bacterium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.79 purified recombinant wild-type and selenomethionine-labeled enzyme, mixing of 0.001 ml of protein solution and 0.001 ml of reservoir solution, method optimization, X-ray diffraction structure determination and analysis at 1.49 A resolution uncultured bacterium

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.79 additional information crosslinking of purified recombinant enzyme by glutaraldehyde, the enzyme aggragates show increased stability compared to free enzyme uncultured bacterium

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.79 uncultured bacterium Q4TZQ3 identified from a metagenomic library by functional screening
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.79 recombinant His-tagged enzyme by nickel affinity chromatography, gel filtration, and ultrafiltration uncultured bacterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.79 4-methylumbelliferyl acetate + H2O
-
 uncultured bacterium 4-methylumbelliferol + acetate
-
 ?
3.1.1.79 4-nitrophenyl acetate + H2O
-
 uncultured bacterium 4-nitrophenol + acetate
-
 ?
3.1.1.79 4-nitrophenyl butyrate + H2O
-
 uncultured bacterium 4-nitrophenol + butyrate
-
 ?
3.1.1.79 additional information the enzyme shows broad substrate specificity, with a strong preference towards short-chain esters, e.g. 4-nitrophenyyl acetateand 4-nitrophenyyl butyrate, little activity is observed towards long-chain esters such as 4-nitrophenyl dodecanoate uncultured bacterium ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.79 dimer four molecules in the asymmetric unit of the enzyme are arranged as a dimer of dimers, the enzyme exhibits an alpha/beta-hydrolase fold consisting of a central beta-sheet enclosed by alpha-helices on both sides uncultured bacterium

Synonyms

EC Number Synonyms Comment Organism
3.1.1.79 Est25
-
 uncultured bacterium
3.1.1.79 HSL
-
 uncultured bacterium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.79 22
-
 assay at uncultured bacterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.79 8
-
 assay at uncultured bacterium

General Information

EC Number General Information Comment Organism
3.1.1.79 additional information the enzyme contains a catalytic Ser201 and the other two catalytic residues Asp303 and His333, that perfectly match to corresponding residues in proteins within the HSL family uncultured bacterium