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Literature summary for 3.5.1.1 extracted from

  • Tomar, R.; Sharma, P.; Srivastava, A.; Bansal, S.; Kundu, A.; Kundu, B.
    Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains (2014), Acta Crystallogr. Sect. D, 70, 3187-3197.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8TZE8
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-

Purification (Commentary)

Purification (Comment) Organism
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Pyrococcus furiosus

Subunits

Subunits Comment Organism
dimer the linker of the two-domain dimeric enzyme is found to be dispensable. Domains of this enzyme assemble without the linker into a conjoined tetrameric form that exhibits higher activity than the parent enzyme.The global shape and quaternary structure of the conjoined enzyme are also similar to the wild-type enzyme, as observed by their solution scattering profiles and X-ray crystallographic data. Comparison of the crystal structures of substrate-bound and unbound enzymes reveal an altogether new active-site composition and mechanism of action Pyrococcus furiosus