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Literature summary for 5.4.2.8 extracted from

  • Regni, C.; Schramm, A.M.; Beamer, L.J.
    The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme (2006), J. Biol. Chem., 281, 15564-15571.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
N110A no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type Pseudomonas aeruginosa
R15A no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type Pseudomonas aeruginosa
R20A no catalytic activity Pseudomonas aeruginosa
R241C 0.3% of wild-type acivity, with Km value similar to wild-type Pseudomonas aeruginosa
R247A no remarkable differences in Km and Vmax value compared to wild-type, modest increase in dissociation of intermediate glucose-1,6-bisphosphate from enzyme Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0127
-
alpha-D-glucose 1-phosphate mutant RN110A Pseudomonas aeruginosa
0.0132
-
alpha-D-glucose 1-phosphate mutant R15A Pseudomonas aeruginosa
0.0195
-
alpha-D-glucose 1-phosphate mutant R247A Pseudomonas aeruginosa
0.0273
-
alpha-D-glucose 1-phosphate wild-type Pseudomonas aeruginosa
0.0279
-
alpha-D-glucose 1-phosphate mutant R421C Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
bifunctional phosphomannomutase/phosphoglucomutase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-glucose 1-phosphate
-
Pseudomonas aeruginosa alpha-D-glucose 6-phosphate
-
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