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Literature summary extracted from
- 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
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 5.5.1.4 | pharmacology | the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs | Homo sapiens |
| 5.5.1.4 | pharmacology | the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs | Saccharomyces cerevisiae |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.5.1.4 | gene INO1, DNA sequence analysis, expression in Saccharomyces cerevisiae | Homo sapiens |
| 5.5.1.4 | gene INO1, DNA sequence analysis, expression is regulated by inositol and Opi1p, phylogenetic analysis | Saccharomyces cerevisiae |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.5.1.4 | additional information | the enzyme-deficient ino1 mutant strain can be functionally complemented by expression of the human enzyme | Saccharomyces cerevisiae |
| 5.5.1.4 | additional information | the human enzyme can functionally complement the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.5.1.4 | 2-deoxy-glucitol-6-phosphate | the inhibitor induces folding of the catalytic domain | Saccharomyces cerevisiae |  |
| 5.5.1.4 | choline | slight inhibition | Saccharomyces cerevisiae | |
| 5.5.1.4 | Inositol | feedback/product inhibition by inhibition of INO1 gene transcription, acts as a metabolic sensor | Saccharomyces cerevisiae | |
| 5.5.1.4 | lithium | - |
Homo sapiens | |
| 5.5.1.4 | lithium | - |
Saccharomyces cerevisiae | |
| 5.5.1.4 | Valproate | noncompetitive, specific, only in vivo, e.g. in brain post mortem, no inhibition of the purified rcombinant enzyme in vitro | Homo sapiens | |
| 5.5.1.4 | Valproate | - |
Saccharomyces cerevisiae | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.5.1.4 | NH4+ | strong activation | Homo sapiens | |
| 5.5.1.4 | NH4+ | strong activation | Saccharomyces cerevisiae | |
| 5.5.1.4 | NH4+ | strong activation | Mycobacterium tuberculosis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.5.1.4 | 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 | - |
? | |
| 5.5.1.4 | 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 | - |
? | |
| 5.5.1.4 | 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 | - |
? | |
| 5.5.1.4 | additional information | Homo sapiens | inositol phosphates are involved in several signal transduction pathways | ? | - |
? | |
| 5.5.1.4 | additional information | Saccharomyces cerevisiae | inositol phosphates are involved in several signal transduction pathways | ? | - |
? | |
| 5.5.1.4 | additional information | Mycobacterium tuberculosis | inositol phosphates are involved in several signal transduction pathways | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.5.1.4 | Homo sapiens | - |
- |
- |
| 5.5.1.4 | Mycobacterium tuberculosis | - |
- |
- |
| 5.5.1.4 | Saccharomyces cerevisiae | - |
gene INO1 | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate | catalytic reaction mechanism | Homo sapiens | |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate | catalytic reaction mechanism, induced-fit active site formation by substrate binding | Saccharomyces cerevisiae | |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate | catalytic reaction mechanism, induced-fit active site formation by substrate binding | Mycobacterium tuberculosis |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 5.5.1.4 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.5.1.4 | 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 | - |
? | |
| 5.5.1.4 | 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 | - |
? | |
| 5.5.1.4 | 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 | - |
? | |
| 5.5.1.4 | D-glucose 6-phosphate | reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+ | Homo sapiens | 1D-myo-inositol 3-phosphate | - |
? | |
| 5.5.1.4 | D-glucose 6-phosphate | reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+ | Saccharomyces cerevisiae | 1D-myo-inositol 3-phosphate | - |
? | |
| 5.5.1.4 | D-glucose 6-phosphate | reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+ | Mycobacterium tuberculosis | 1D-myo-inositol 3-phosphate | - |
? | |
| 5.5.1.4 | additional information | inositol phosphates are involved in several signal transduction pathways | Homo sapiens | ? | - |
? | |
| 5.5.1.4 | additional information | inositol phosphates are involved in several signal transduction pathways | Saccharomyces cerevisiae | ? | - |
? | |
| 5.5.1.4 | additional information | inositol phosphates are involved in several signal transduction pathways | Mycobacterium tuberculosis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.5.1.4 | More | the protomer contains 2 domains, a Rossman fold with a C-terminal extension D1a, and a domain involving tetramerization D1b | Mycobacterium tuberculosis |
| 5.5.1.4 | More | the protomer contains 3 domains, a catalytic domain, a central domain, and an NAD+ binding domain | Saccharomyces cerevisiae |
| 5.5.1.4 | tetramer | homotetramer formed by dimerization of dimers | Saccharomyces cerevisiae |
| 5.5.1.4 | tetramer | homotetramer formed by dimerization of dimers | Mycobacterium tuberculosis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.5.1.4 | 1D-myo-inositol 3-phosphate synthase | - |
Homo sapiens |
| 5.5.1.4 | 1D-myo-inositol 3-phosphate synthase | - |
Saccharomyces cerevisiae |
| 5.5.1.4 | 1D-myo-inositol 3-phosphate synthase | - |
Mycobacterium tuberculosis |
| 5.5.1.4 | MIP synthase | - |
Homo sapiens |
| 5.5.1.4 | MIP synthase | - |
Saccharomyces cerevisiae |
| 5.5.1.4 | MIP synthase | - |
Mycobacterium tuberculosis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.5.1.4 | NAD+ | dependent on | Homo sapiens | |
| 5.5.1.4 | NAD+ | dependent on | Saccharomyces cerevisiae | |
| 5.5.1.4 | NAD+ | dependent on | Mycobacterium tuberculosis | |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.5.1.4 | 0.21 | - |
Valproate | brain, post mortem | Homo sapiens | |
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Release 2023.1 (January 2023)
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