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Structural insight into a CE15 esterase from the marine bacterial metagenome
(Journal article; Tidsskriftartikkel; Peer reviewed, 2017-12-08)
The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-characterized fungal homologs, and resolves three large loop regions that are unique to this bacterial ...
Biochemical characterization of a family 15 carbohydrate esterase from a bacterial marine Arctic metagenome
(Journal article; Tidsskriftartikkel; Peer reviewed, 2016)
Background
The glucuronoyl esterase enzymes of wood-degrading fungi (Carbohydrate Esterase family 15; CE15) form part of the hemicellulolytic and cellulolytic enzyme systems that break down plant biomass, and have possible applications in biotechnology. Homologous enzymes are predicted in the genomes of several bacteria, however these have been much less studied than their fungal counterparts. ...
Complete genome sequence of Halomonas sp. R5-57
(Journal article; Tidsskriftartikkel; Peer reviewed, 2016)
The marine Arctic isolate Halomonas sp. R5-57 was sequenced as part of a bioprospecting project which aims to
discover novel enzymes and organisms from low-temperature environments, with potential uses in biotechnological
applications. Phenotypically, Halomonas sp. R5-57 exhibits high salt tolerance over a wide range of temperatures and
has extra-cellular hydrolytic activities with several ...
Recombinant expression and purification of an ATP-dependent DNA ligase from Aliivibrio salmonicida
(Journal article; Tidsskriftartikkel; Peer reviewed, 2014-05)
The genome of the psychrophilic fish-pathogen Aliivibrio salmonicida encodes a putative ATP-dependent DNA ligase in addition to a housekeeping NAD-dependent enzyme. In order to study the structure and activity of the ATP dependent ligase in vitro we have undertaken its recombinant production and purification from an Escherichia coli based expression system.
Expression and purification of this ...
High quality draft genome sequence of Streptomyces sp. strain AW19M42 isolated from a sea squirt in Northern Norway
(Journal article; Tidsskriftartikkel; Peer reviewed, 2014)
Enzyme-adenylate structure of a bacterial ATP-dependent DNA ligase with a minimized DNA-binding surface
(Journal article; Tidsskriftartikkel; Peer reviewed, 2014-11-01)
DNA ligases are a structurally diverse class of enzymes which
share a common catalytic core and seal breaks in the
phosphodiester backbone of double-stranded DNA via an
adenylated intermediate. Here, the structure and activity of a
recombinantly produced ATP-dependent DNA ligase from
the bacterium Psychromonas sp. strain SP041 is described.
This minimal-type ligase, like its close homologues, ...
Cold shock induction of recombinant Arctic environmental genes
(Journal article; Tidsskriftartikkel; Peer reviewed, 2015-08-19)
Background: Heterologous expression of psychrophilic enzymes in E. coli is particularly challenging due to their intrinsic instability. The low stability is regarded as a consequence of adaptation that allow them to function at low temperatures. Recombinant production presents a significant barrier to their exploitation for commercial applications in industry.
<p>Methods: As part of an enzyme ...
Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds
(Journal article; Tidsskriftartikkel; Peer reviewed, 2020-05-04)
DNA ligases are diverse enzymes with essential functions in replication and repair of DNA; here we review recent advances in their structure and distribution and discuss how this contributes to understanding their biological roles and technological potential. Recent high-resolution crystal structures of DNA ligases from different organisms, including DNA-bound states and reaction intermediates, have ...
DNA binding with a minimal scaffold: structure-function analysis of Lig E DNA ligases
(Journal article; Tidsskriftartikkel; Peer reviewed, 2018-07-11)
DNA ligases join breaks in the phosphodiester backbone of DNA by catalysing the formation of bonds between opposing 5′P and 3′OH ends in an adenylation-dependent manner. Catalysis is accompanied by reorientation of two core domains to provide access to the active site for cofactor utilization and enable substrate binding and product release. The general paradigm is that DNA ligases engage their DNA ...
Biochemical characterization of ParI, an orphan C5-DNA methyltransferase from Psychrobacter arcticus 273-4
(Journal article; Tidsskriftartikkel; Peer reviewed, 2018-05-25)
<p>Cytosine-specific DNA methyltransferases are important enzymes in most living organisms. In prokaryotes, most DNA methyltransferases are members of the type II restriction-modification system where they methylate host DNA, thereby protecting it from digestion by the accompanying restriction endonucleases. DNA methyltransferases can also act as solitary enzymes having important roles in controlling ...