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Literature summary for 5.4.2.6 extracted from

  • Griffin, J.L.; Bowler, M.W.; Baxter, N.J.; Leigh, K.N.; Dannatt, H.R.; Hounslow, A.M.; Blackburn, G.M.; Webster, C.E.; Cliff, M.J.; Waltho, J.P.
    Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate (2012), Proc. Natl. Acad. Sci. USA, 109, 6910-6915.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme in complex with transition-state analogue fluoromagnesate and glucose 6-phosphate or ground-state analogue fluoroaluminate and glucose 6-phosphate, sitting drop vapour diffusion method, mixing of 15 mg/mL 50 mM K+ HEPES, pH 7.2, 5 mM MgCl2, 1 mM azide, 0.1 mM DTT, 10 mM NH4F, and 10 mM BeCl2 1:1 with the precipitant containing 26-30% w/v PEG 4000, 200 mM Na acetate, and 100 mM Tris, pH 7.5, X-ray diffraction structure determination and analysis at 1.65 A resolution, molecular replacement Lactococcus lactis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-D-Glucose 1-phosphate Lactococcus lactis
-
beta-D-Glucose 6-phosphate
-
r

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-Glucose 1-phosphate
-
Lactococcus lactis beta-D-Glucose 6-phosphate
-
r

Synonyms

Synonyms Comment Organism
beta-PGM
-
Lactococcus lactis

General Information

General Information Comment Organism
additional information fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase demonstrate the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes, overview Lactococcus lactis