Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.5.1.4 extracted from

  • Ju, S.; Greenberg, M.L.
    1D-myo-inositol 3-phosphate synthase: conservation, regulation, and putative target of mood stabilizers (2004), Clin. Neurosci. Res., 4, 181-187.
No PubMed abstract available

Application

Application Comment Organism
pharmacology the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs Homo sapiens
pharmacology the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
gene INO1, DNA sequence analysis, expression in Saccharomyces cerevisiae Homo sapiens
gene INO1, DNA sequence analysis, expression is regulated by inositol and Opi1p, phylogenetic analysis Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information the enzyme-deficient ino1 mutant strain can be functionally complemented by expression of the human enzyme Saccharomyces cerevisiae
additional information the human enzyme can functionally complement the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2-deoxy-glucitol-6-phosphate the inhibitor induces folding of the catalytic domain Saccharomyces cerevisiae
choline slight inhibition Saccharomyces cerevisiae
Inositol feedback/product inhibition by inhibition of INO1 gene transcription, acts as a metabolic sensor Saccharomyces cerevisiae
lithium
-
Homo sapiens
lithium
-
Saccharomyces cerevisiae
Valproate noncompetitive, specific, only in vivo, e.g. in brain post mortem, no inhibition of the purified rcombinant enzyme in vitro Homo sapiens
Valproate
-
Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
NH4+ strong activation Homo sapiens
NH4+ strong activation Saccharomyces cerevisiae
NH4+ strong activation Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose 6-phosphate Homo sapiens the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview 1D-myo-inositol 3-phosphate
-
?
D-glucose 6-phosphate Saccharomyces cerevisiae the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview 1D-myo-inositol 3-phosphate
-
?
D-glucose 6-phosphate Mycobacterium tuberculosis the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview 1D-myo-inositol 3-phosphate
-
?
additional information Homo sapiens inositol phosphates are involved in several signal transduction pathways ?
-
?
additional information Saccharomyces cerevisiae inositol phosphates are involved in several signal transduction pathways ?
-
?
additional information Mycobacterium tuberculosis inositol phosphates are involved in several signal transduction pathways ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mycobacterium tuberculosis
-
-
-
Saccharomyces cerevisiae
-
gene INO1
-

Reaction

Reaction Comment Organism Reaction ID
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate catalytic reaction mechanism Homo sapiens
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate catalytic reaction mechanism, induced-fit active site formation by substrate binding Saccharomyces cerevisiae
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate catalytic reaction mechanism, induced-fit active site formation by substrate binding Mycobacterium tuberculosis

Source Tissue

Source Tissue Comment Organism Textmining
additional information the enzyme activity is maximal during the logarithmic stage of growth and is decreased in the stationary phase Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose 6-phosphate the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview Homo sapiens 1D-myo-inositol 3-phosphate
-
?
D-glucose 6-phosphate the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview Saccharomyces cerevisiae 1D-myo-inositol 3-phosphate
-
?
D-glucose 6-phosphate the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview Mycobacterium tuberculosis 1D-myo-inositol 3-phosphate
-
?
D-glucose 6-phosphate reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+ Homo sapiens 1D-myo-inositol 3-phosphate
-
?
D-glucose 6-phosphate reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+ Saccharomyces cerevisiae 1D-myo-inositol 3-phosphate
-
?
D-glucose 6-phosphate reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+ Mycobacterium tuberculosis 1D-myo-inositol 3-phosphate
-
?
additional information inositol phosphates are involved in several signal transduction pathways Homo sapiens ?
-
?
additional information inositol phosphates are involved in several signal transduction pathways Saccharomyces cerevisiae ?
-
?
additional information inositol phosphates are involved in several signal transduction pathways Mycobacterium tuberculosis ?
-
?

Subunits

Subunits Comment Organism
More the protomer contains 2 domains, a Rossman fold with a C-terminal extension D1a, and a domain involving tetramerization D1b Mycobacterium tuberculosis
More the protomer contains 3 domains, a catalytic domain, a central domain, and an NAD+ binding domain Saccharomyces cerevisiae
tetramer homotetramer formed by dimerization of dimers Saccharomyces cerevisiae
tetramer homotetramer formed by dimerization of dimers Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
1D-myo-inositol 3-phosphate synthase
-
Homo sapiens
1D-myo-inositol 3-phosphate synthase
-
Saccharomyces cerevisiae
1D-myo-inositol 3-phosphate synthase
-
Mycobacterium tuberculosis
MIP synthase
-
Homo sapiens
MIP synthase
-
Saccharomyces cerevisiae
MIP synthase
-
Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NAD+ dependent on Homo sapiens
NAD+ dependent on Saccharomyces cerevisiae
NAD+ dependent on Mycobacterium tuberculosis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.21
-
Valproate brain, post mortem Homo sapiens