Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Zhang, G.; Dai, J.; Wang, L.; Dunaway-Mariano, D.; Tremblay, L.W.; Allen, K.N.
    Catalytic cycling in beta-phosphoglucomutase: a kinetic and structural analysis (2005), Biochemistry, 44, 9404-9416.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.2.6 in complex with Mg2+ Lactococcus lactis

Protein Variants

EC Number Protein Variants Comment Organism
5.4.2.6 D170A 700fold reduction of kcat-value Lactococcus lactis
5.4.2.6 D8A no catalytic activity Lactococcus lactis
5.4.2.6 D8E no catalytic activity Lactococcus lactis
5.4.2.6 E169A/D170A 1400fold reduction of kcat-value Lactococcus lactis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.2.6 0.0078
-
beta-D-glucose 1-phosphate mutant D170A, 25°C, pH 7.0 Lactococcus lactis
5.4.2.6 0.0146
-
beta-D-glucose 1-phosphate wild-type, 25°C, pH 7.0 Lactococcus lactis
5.4.2.6 0.39
-
beta-D-glucose 1-phosphate mutant E169A/D170A, 25°C, pH 7.0 Lactococcus lactis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.2.6 Mg2+ Km-value 0.270 mM Lactococcus lactis

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.6 Lactococcus lactis P71447
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.2.6 beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate a single Mg2+ coordination site accomodates water, phosphate, and the phosphorane intermediate during catalytic turnover. Bi-bi ping-pong mechanism, substrate induced-fit mechanism allows phosphomutase activity to dominate over the intrinsic phosphatase activity Lactococcus lactis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.2.6 beta-D-Glucose 1-phosphate
-
Lactococcus lactis beta-D-Glucose 6-phosphate
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.4.2.6 0.0012
-
beta-D-glucose 1-phosphate mutant E169A/D170A, 25°C, pH 7.0 Lactococcus lactis
5.4.2.6 0.00384
-
beta-D-glucose 1-phosphate mutant D170A, 25°C, pH 7.0 Lactococcus lactis
5.4.2.6 17.1
-
beta-D-glucose 1-phosphate wild-type, 25°C, pH 7.0 Lactococcus lactis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.2.6 7
-
-
Lactococcus lactis