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Literature summary extracted from

  • Andreotti, G.; Monti, M.C.; Citro, V.; Cubellis, M.V.
    Heterodimerization of two pathological mutants enhances the activity of human phosphomannomutase2 (2015), PLoS ONE, 10, e0139882 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.2.8 D-Glucose 1,6-bisphosphate
-
 Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.2.8 expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
5.4.2.8 F119L the mutant shows reduced activity compared to the wild type enzyme Homo sapiens
5.4.2.8 R141H inactive Homo sapiens
5.4.2.8 R141H/F119L the stability-impaired mutant has wild type activity Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.8 Homo sapiens O15305
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.4.2.8 fibroblast
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.2.8 alpha-D-glucose 1-phosphate
-
 Homo sapiens D-glucose 6-phosphate
-
 ?
5.4.2.8 alpha-D-mannose 1-phosphate
-
 Homo sapiens D-mannose 6-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.4.2.8 ? x * 27950, electrospray ionization mass spectrometry Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
5.4.2.8 phosphomannomutase 2
-
 Homo sapiens
5.4.2.8 PMM2
-
 Homo sapiens