Epi-Inositol

Last updated
epi-Inositol
Epi-inositol.svg
Names
IUPAC name
epi-Inositol [1]
Preferred IUPAC name
(1R,2R,3r,4S,5S,6s)-Cyclohexane-1,2,3,4,5,6-hexol
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
ECHA InfoCard 100.006.984 OOjs UI icon edit-ltr-progressive.svg
UNII
  • InChI=1S/C6H12O6/c7-1-2(8)4(10)6(12)5(11)3(1)9/h1-12H/t1-,2-,3-,4+,5-,6+ Yes check.svgY
    Key: CDAISMWEOUEBRE-NIPYSYMMSA-N Yes check.svgY
  • O[C@H]1[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H]1O
Properties
C6H12O6
Molar mass 180.156 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Yes check.svgY  verify  (what is  Yes check.svgYX mark.svgN ?)

Epi-Inositol is one of the stereoisomers of inositol. [2]

Contents

Use in medicine

Epi-inositol has been found to regulate Yeast INO1 Gene Encoding (Inositol-1-P synthase) in animals. During the study with Epi-Inositol, Yeast INO1-expression was measured in northern blots. [3]

See also

Related Research Articles

Inositol Carbocyclic sugar

Inositol, or more precisely myo-inositol, is a carbocyclic sugar that is abundant in the brain and other mammalian tissues; it mediates cell signal transduction in response to a variety of hormones, neurotransmitters, and growth factors and participates in osmoregulation.

V-ATPase Family of transport protein complexes

Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pumps protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.

Aldosterone synthase Protein-coding gene in the species Homo sapiens

Aldosterone synthase, also called steroid 18-hydroxylase, corticosterone 18-monooxygenase or P450C18, is a steroid hydroxylase cytochrome P450 enzyme involved in the biosynthesis of the mineralocorticoid aldosterone and other steroids. The enzyme catalyzes sequential hydroxylations of the steroid angular methyl group at C18 after initial 11β-hydroxylation. It is encoded by CYP11B2 gene in humans.

Fatty acid synthase

Fatty acid synthase (FAS) is an enzyme that in humans is encoded by the FASN gene.

Acetolactate synthase Class of enzymes

The acetolactate synthase (ALS) enzyme is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids.

Cystathionine beta synthase Mammalian protein found in Homo sapiens

Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. It catalyzes the first step of the transsulfuration pathway, from homocysteine to cystathionine:

1<small>D</small>-<i>chiro</i>-Inositol Chemical compound

1D-chiro-Inositol is a member of a family of related substances often referred to collectively as "inositol", although that term encompasses several isomers of questionable biological relevance, including 1L-chiro-inositol. myo-Inositol is converted into DCI by an insulin dependent NAD/NADH epimerase enzyme. It is known to be an important secondary messenger in insulin signal transduction. DCI accelerates the dephosphorylation of glycogen synthase and pyruvate dehydrogenase, rate limiting enzymes of non-oxidative and oxidative glucose disposal. DCI may act to bypass defective normal epimerization of myo-inositol to DCI associated with insulin resistance and at least partially restore insulin sensitivity and glucose disposal. One pilot study found males taking it had increased androgens and reduced estrogen.

Prostaglandin D<sub>2</sub> synthase Protein-coding gene in the species Homo sapiens

Prostaglandin-H2 D-isomerase (PTGDS) is an enzyme that in humans is encoded by the PTGDS gene.

PRKCB1

Protein kinase C beta type is an enzyme that in humans is encoded by the PRKCB gene.

Serine/threonine-protein kinases SGK represent a kinase subfamily with orthologs found across animal clades and in yeast. In most vertebrates, including humans, there are three isoforms encoded by the genes SGK1, SGK2, and SGK3. The name Serum/glucocorticoid-regulated kinase refers to the first cloning of a SGK family member from a cDNA library screen for genes upregulated by the glucocorticoid dexamethasone in a rat mammary epithelial tumor cell line. The first human family member was cloned in a screen of hepatocellular genes regulated in response to cellular hydration or swelling.

ITPR1

Inositol 1,4,5-trisphosphate receptor type 1 is a protein that in humans is encoded by the ITPR1 gene.

Inositol-3-phosphate synthase

In enzymology, an inositol-3-phosphate synthase is an enzyme that catalyzes the chemical reaction

PTGS1

Cyclooxygenase 1 (COX-1), also known as prostaglandin G/H synthase 1, prostaglandin-endoperoxide synthase 1 or prostaglandin H2 synthase 1, is an enzyme that in humans is encoded by the PTGS1 gene. In humans it is one of two cyclooxygenases.

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<i>neo</i>-Inositol Chemical compound

neo-Inositol is one of the stereoisomers of inositol. It is one of the nine isomeric forms of cyclohexanehexol; a group of small and chemically very stable polar molecules that have versatile properties. This stereoisomer is naturally occurring, but only in small amounts. It is also known as (1s,2R,3R,4s,5S,6S)-cyclohexane-1,2,3,4,5,6-hexol or 1,2,3/4,5,6-cyclohexanehexol in the IUPAC naming system.

1<small>L</small>-<i>chiro</i>-Inositol Chemical compound

1L-chiro-Inositol (L-chiro-Inositol) is one of the isomers of inositol.

<i>cis</i>-Inositol Chemical compound

cis-Inositol is one of the isomers of inositol.

<i>allo</i>-Inositol Chemical compound

allo-Inositol is a stereoisomer of inositol.

An upstream activating sequence or upstream activation sequence (UAS) is a cis-acting regulatory sequence. It is distinct from the promoter and increases the expression of a neighbouring gene. Due to its essential role in activating transcription, the upstream activating sequence is often considered to be analogous to the function of the enhancer in multicellular eukaryotes. Upstream activation sequences are a crucial part of induction, enhancing the expression of the protein of interest through increased transcriptional activity. The upstream activation sequence is found adjacently upstream to a minimal promoter and serves as a binding site for transactivators. If the transcriptional transactivator does not bind to the UAS in the proper orientation then transcription cannot begin. To further understand the function of an upstream activation sequence, it is beneficial to see its role in the cascade of events that lead to transcription activation. The pathway begins when activators bind to their target at the UAS recruiting a mediator. A TATA-binding protein subunit of a transcription factor then binds to the TATA box, recruiting additional transcription factors. The mediator then recruits RNA polymerase II to the pre-initiation complex. Once initiated, RNA polymerase II is released from the complex and transcription begins.

Ceramide synthase 1 Protein-coding gene in the species Homo sapiens

Ceramide synthase 1 also known as LAG1 longevity assurance homolog 1 is an enzyme that in humans is encoded by the CERS1 gene.

References

  1. ↑ International Union of Pure and Applied Chemistry (2014). Nomenclature of Organic Chemistry: IUPAC Recommendations and Preferred Names 2013. The Royal Society of Chemistry. p. 1415. doi:10.1039/9781849733069. ISBN   978-0-85404-182-4.
  2. ↑ "Inositols". ursula.chem.yale.edu. Retrieved 2022-06-17.
  3. ↑ A., Shaldubina; S., Ju; L., Vaden; D, Ding; Belmaker, R. H; Greenberg, M. L (February 13, 2002). "Epi-inositol regulates expression of the yeast INO1 gene encoding inositol-1-P synthase". Millipore Sigma. PMID   11840310. Archived from the original on June 17, 2022. Retrieved June 17, 2022.


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