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Literature summary for 5.4.2.2 extracted from

  • Nogly, P.; Castro, R.; de Rosa, M.; Neves, A.R.; Santos, H.; Archer, M.
    Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis (2012), Acta Crystallogr. Sect. F, 68, 1113-1115.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloned and homologously overexpressed in Lactococcus lactis subsp. cremoris strain NZ9000, introducing 6xHis-tag Lactococcus lactis

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallized with vapor diffusion, streak seeding, in ammonium sulfate solution, optimized crystals diffract to 1.5 A resolution Lactococcus lactis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29880
-
calculated Lactococcus lactis
30000
-
SDS-PAGE of purified alpha-PGM, with His-tag Lactococcus lactis

Organism

Organism UniProt Comment Textmining
Lactococcus lactis Q00G41
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein is purified by centrifugation und affinity chromatography with Ni-NTA Superflow cartridge. Purity is assessed by SDS-PAGE Lactococcus lactis

Storage Stability

Storage Stability Organism
-80°C, fast-frozen in LN2 and stored for 2 years without affecting the sample homogeneity Lactococcus lactis

Synonyms

Synonyms Comment Organism
alpha-Pgm
-
Lactococcus lactis
alpha-phosphoglucomutase
-
Lactococcus lactis

General Information

General Information Comment Organism
physiological function Unlike the majority of alpha-phosphoglucomutases, the described enzyme of 252 residues with alpha-phosphoglucomutase activity, is related to eukaryotic phosphomannomutases and belongs to HAD-superfamily hydrolase, subfamily IIB. Lactococcus lactis