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Literature summary extracted from

  • May, T.B.; Shinabarger, D.; Boyd, A.; Chakrabarty, A.M.
    Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa (1994), J. Biol. Chem., 269, 4872-4877.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.13 expression of wild-type and several PMI-GMP mutants in algA mutant 8853 Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.13 K175E approx. 9% of wild-type activity, 600fold increase in Km for mannose 1-phosphate Pseudomonas aeruginosa
2.7.7.13 K175Q approx. 40% of wild-type activity, 3200fold increase in Km for mannose 1-phosphate Pseudomonas aeruginosa
2.7.7.13 K175R 470fold increase in mannose 1-phosphate Km value Pseudomonas aeruginosa
2.7.7.13 K20Q enzyme is unable to support alginate synthesis although it shows no significant differences in Vmax and Km as compared to wild-type Pseudomonas aeruginosa
2.7.7.13 R19H approx. 50% of wild-type activity, 8fold increase in Km for mannose 1-phosphate Pseudomonas aeruginosa
2.7.7.13 R19K approx. 50% of wild-type activity, 2 and 6fold increase in Km for mannose 1-phosphate and GTP, respectively Pseudomonas aeruginosa
2.7.7.13 R19L approx. 50% of wild-type activity, 5fold increase in Km for mannose 1-phosphate and GTP, respectively Pseudomonas aeruginosa
2.7.7.13 S12A approx. 44% of wild-type activity, 2 and 3fold decrease in Km for mannose 1-phosphate and GTP, respectively Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.13 0.0082
-
 alpha-D-mannose 1-phosphate 25°C, cosubstrate GTP Pseudomonas aeruginosa
2.7.7.13 0.041
-
 GTP 25°C, cosubstrate mannose 1-phosphate Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.13 GTP + alpha-D-mannose 1-phosphate Pseudomonas aeruginosa
-
 GDPmannose + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.13 Pseudomonas aeruginosa P07874 enzyme is encoded by the algA gene
-
5.3.1.8 Pseudomonas aeruginosa
-
 bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.13
-
 Pseudomonas aeruginosa

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.7.13 GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose PMI and GMP activities are most probably located in catalytically distinct domains Pseudomonas aeruginosa
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.13 GTP + alpha-D-mannose 1-phosphate
-
 Pseudomonas aeruginosa GDPmannose + diphosphate
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate
-
 Pseudomonas aeruginosa diphosphate + GDP-mannose
-
 ?
5.3.1.8 D-Mannose 6-phosphate
-
 Pseudomonas aeruginosa D-Fructose 6-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.1.8 More bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is composed of two independent enzymatic domains. The carboxyl terminus is critical for mannose-6-phosphate isomerase Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
2.7.7.13 PIM-GMP
-
-