ArticleInternational journal of biochemistry and molecular biology2012
Site-directed mutagenesis of a family 42 β-galactosidase from an antarctic bacterium.
Article in International journal of biochemistry and molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- A New β-Galactosidase from the Antarctic Bacterium Alteromonas sp. ANT48 and Its Potential in Formation of Prebiotic Galacto-Oligosaccharides.Marine drugs · 2019Article
- Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the β-galactosidase from Bacillus subtilis VTCC-DVN-12-01.BMC biochemistry · 2016Article
- Amino acid substitutions in cold-adapted proteins from Halorubrum lacusprofundi, an extremely halophilic microbe from antarctica.PloS one · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Site directed mutagenesis was used to modify the active site of a cold active beta-galactosidase taken from an Antarctic psychrotolerant Planococcus Bacterial isolate. The goal was to modify the active site such that there would be an increase in activity on certain substrates which showed little to no activity with the wild type enzyme. A total of 5 mutant enzymes were constructed with amino acid changes based on an analysis done via homology modeling. All 5 modified enzymes were assayed using 14 different nitrophenol substrates. In most cases there was a loss of activity on substrates that showed activity with the wild type enzymes. None of the expected activity was observed with any of the mutants, possibly in part due to a decrease in hydrogen bonding between the active site and the substrates. With the substrates p-nitrophenyl-β-d-galacturonide and p-nitrophenyl-α-d-glucopyranoside we saw increased activity. With one of the mutants we measured a 320% increase in activity on p-nitrophenyl-β-d-galacturonide. Two other mutants showed activity on p-nitrophenyl-α-d-glucopyranoside, which showed no activity at all with the wild type enzyme.
Indexed as
Identifiers
22773960PMC3388732W258580054What OpenQuestion holds
Registered trials
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