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Literature summary for 5.4.2.8 extracted from

  • Jackson, S.A.; Duan, M.; Zhang, P.; Ihua, M.W.; Stengel, D.B.; Duan, D.; Dobson, A.D.W.
    Isolation, identification, and biochemical characterization of a novel bifunctional phosphomannomutase/phosphoglucomutase from the metagenome of the brown alga Laminaria digitata (2022), Front. Microbiol., 13, 1000634.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-Glucose 1,6-bisphosphate 0.1 mM used in assay conditions Laminaria digitata

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Laminaria digitata

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ has a negative effect on phosphomannomutase activity relative to the control Laminaria digitata
Co2+ has a negative effect on phosphomannomutase activity relative to the control Laminaria digitata
Li2+ has a negative effect on phosphomannomutase activity relative to the control Laminaria digitata
Na+ has a negative effect on phosphomannomutase activity relative to the control Laminaria digitata
NaCl both the enzyme's phosphoglucomutase and phosphomannomutase activities decrease at increased NaCl concentrations, with phosphomannomutase displaying slightly higher levels of relative activity (55% relative activity at 0.2 M NaCl) than phosphoglucomutase (43% relative activity at 0.2 M); but as NaCl concentrations increase, similar decreases in relative phosphoglucomutase and phosphomannomutase activities are evident Laminaria digitata

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ promotes both phosphoglucomutase and phosphomannomutase activities of the enzyme. 10 mM is used in assay conditions Laminaria digitata
Mn2+ enhances the phosphoglucomutase activity of the enzyme Laminaria digitata
Zn2+ enhances the phosphoglucomutase activity of the enzyme Laminaria digitata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha-D-glucose 1-phosphate Laminaria digitata
-
D-glucose 6-phosphate
-
?
alpha-D-mannose 1-phosphate Laminaria digitata
-
D-mannose 6-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Laminaria digitata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
maltose-binding protein Trap column chromatography and Superdex 200 gel filtration Laminaria digitata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-glucose 1-phosphate
-
Laminaria digitata D-glucose 6-phosphate
-
?
alpha-D-mannose 1-phosphate
-
Laminaria digitata D-mannose 6-phosphate
-
?

Subunits

Subunits Comment Organism
? x * 92180, maltose-binding protein-tagged enzyme, SDS-PAGE Laminaria digitata

Synonyms

Synonyms Comment Organism
10L6AlgC bifunctional enzyme with phosphomannomutase/phosphoglucomutase activities Laminaria digitata
PGM
-
Laminaria digitata
PMM
-
Laminaria digitata

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Laminaria digitata

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 50 more than 50% activity between 25 and 50°C Laminaria digitata

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45 70 the enzyme is stable at 45°C, with a reduction in relative phosphoglucomutase activity of 61.36%. 19.7, 7.17, 1.43, and 0.72%, respectively, being observed for every 5°C increase in temperature up to 70°C. In contrast, the phosphomannomutase activity is slightly less influenced by increases in temperature, with relative activities being reduced to 93.84, 51.66, 5.21, 4.98, and 3.79%, respectively, over the sample temperature range Laminaria digitata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Laminaria digitata

pH Range

pH Minimum pH Maximum Comment Organism
7.5 8.5 more than 50% activity between pH 7.5 and 8.5 Laminaria digitata