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Literature summary for 3.1.3.3 extracted from

  • Cho, H.; Wang, W.; Kim, R.; Yokota, H.; Damo, S.; Kim, S.H.; Wemmer, D.; Kustu, S.; Yan, D.
    BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase (2001), Proc. Natl. Acad. Sci. USA, 98, 8525-8530.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are grown by using the hanging drop vapor diffusion method with seeding.1.5 A resolution the X-ray crystal structure of the complex of BeF3 2 with phosphoserine phosphatase. The structure is comparable to that of a phosphoenzyme intermediate: BeF3- is bound to Asp11 with the tetrahedral geometry of a phosphoryl group, is coordinated to Mg2+, and is bound to residues surrounding the active site that are conserved in the haloacid dehalogenase (HAD) superfamily Methanocaldococcus jannaschii

Inhibitors

Inhibitors Comment Organism Structure
BeF3- at 50°C, the hydrolytic activity of is markedly inhibited (more than 95%) in the presence of both BeCl2 and NaF. The latter is provided at concentrations that yield predominantly BeF3- in situ. Either BeCl2 or NaF alone has a much smaller inhibitory effect (35 or 20%, respectively). Similar inhibition by BeF3- is observed at room temperature or at 70°C Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58989
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Methanocaldococcus jannaschii DSM 2661 Q58989
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Synonyms

Synonyms Comment Organism
PSP
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Methanocaldococcus jannaschii