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Literature summary extracted from

  • Kawamura, T.; Watanabe, N.; Tanaka, I.
    Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii (2008), Acta Crystallogr. Sect. D, 64, 1267-1276.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.70 apo enzyme form lacking magnesium ions using the multiple-wavelength anomalous diffraction method and magnesium-bound holo enzyme form using the molecular-replacement method, with 16-20% (w/v) PEG 3350, 0.2 M ammonium chloride and 0.1 M MES-NaOH pH 6.0 Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.70 Pyrococcus horikoshii O58690
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.70 ammonium sulfate precipitation, HiTrap Ni2+-chelating column chromatography, Source 15Q column chromatography, and Superdex 75 gel filtration Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.70 2-(alpha-D-glucosyl)-3-phosphoglycerate + H2O
-
Pyrococcus horikoshii 2-(alpha-D-mannosyl)-D-glycerate + phosphate
-
ir

Synonyms

EC Number Synonyms Comment Organism
3.1.3.70 MPGP
-
Pyrococcus horikoshii