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Literature summary for 5.5.1.4 extracted from

  • Neelon, K.; Wang, Y.; Stec, B.; Roberts, M.F.
    Probing the mechanism of the Archaeoglobus fulgidus inositol-1-phosphate synthase (2005), J. Biol. Chem., 280, 11475-11482.
    View publication on PubMed
Search for more literature for 5.5.1.4

Protein Variants

Protein Variants Comment Organism
D225A site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme Archaeoglobus fulgidus
D332A site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps Archaeoglobus fulgidus
K274A site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme Archaeoglobus fulgidus
K278A site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme Archaeoglobus fulgidus
K306A site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps Archaeoglobus fulgidus
K367A site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme Archaeoglobus fulgidus
L257A site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme Archaeoglobus fulgidus
N255A site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows reduced activity Archaeoglobus fulgidus

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Archaeoglobus fulgidus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-Glucose 6-phosphate Archaeoglobus fulgidus first step in the biosynthesis of the unusual osmolyte di-myo-inositol-1,1'-phosphate L-myo-Inositol 1-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
D-glucose 6-phosphate = L-myo-inositol 1-phosphate substrate binding and metal-dependent reaction mechanism, overview, active site residues are D225, K274, K278, K306, D332, and K367 Archaeoglobus fulgidus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glucose 6-phosphate first step in the biosynthesis of the unusual osmolyte di-myo-inositol-1,1'-phosphate Archaeoglobus fulgidus L-myo-Inositol 1-phosphate
-
 ?
D-Glucose 6-phosphate reaction mechanism involves 3 reaction steps: 1. oxidation by NAD+, 2. condensation to a cyclic molecule, 3. reduction by NADH Archaeoglobus fulgidus L-myo-Inositol 1-phosphate
-
 ?

Synonyms

Synonyms Comment Organism
inositol-1-phosphate synthase
-
 Archaeoglobus fulgidus
MIPS
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
 assay at Archaeoglobus fulgidus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Archaeoglobus fulgidus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Archaeoglobus fulgidus
NADH
-
 Archaeoglobus fulgidus