Inositol-3-phosphate synthase

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inositol-3-phosphate synthase
1gr0.jpg
Inositol-3-phosphate synthase homotetramer, Mycobacterium tuberculosis
Identifiers
EC no. 5.5.1.4
CAS no. 9032-95-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins
Myo-inositol-1-phosphate synthase
PDB 1u1i EBI.jpg
myo-inositol phosphate synthase mips from a. fulgidus
Identifiers
SymbolInos-1-P_synth
Pfam PF01658
InterPro IPR013021
SCOP2 1gr0 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In enzymology, an inositol-3-phosphate synthase (EC 5.5.1.4) is an enzyme that catalyzes the chemical reaction

Contents

D-glucose 6-phosphate 1D-myo-inositol 3-phosphate

Hence, this enzyme has one substrate, D-glucose 6-phosphate, and one product, 1D-myo-inositol 3-phosphate.

This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 1D-myo-inositol-3-phosphate lyase (isomerizing). Other names in common use include myo-inositol-1-phosphate synthase, D-glucose 6-phosphate cycloaldolase, inositol 1-phosphate synthatase, glucose 6-phosphate cyclase, inositol 1-phosphate synthetase, glucose-6-phosphate inositol monophosphate cycloaldolase, glucocycloaldolase, and 1L-myo-inositol-1-phosphate lyase (isomerizing).

This enzyme participates in streptomycin biosynthesis and inositol phosphate metabolism. It employs one cofactor, NAD+. The reaction this enzyme catalyses represents the first committed step in the production of all inositol-containing compounds, including phospholipids, either directly or by salvage. The enzyme exists in a cytoplasmic form in a wide range of plants, animals, and fungi. It has also been detected in several bacteria and a chloroplast form is observed in alga and higher plants. Inositol phosphates play an important role in signal transduction.

In Saccharomyces cerevisiae (Baker's yeast), the transcriptional regulation of the INO1 gene encoding inositol-3-phosphate synthase has been studied in detail and its expression is sensitive to the availability of phospholipid precursors as well as growth phase. [1] The regulation of the structural gene encoding 1L-myo-inositol-1-phosphate synthase has also been analyzed at the transcriptional level in the aquatic angiosperm, Spirodela polyrrhiza (Giant duckweed) and the halophyte, Mesembryanthemum crystallinum (Common ice plant). [2]

In prokaryotes, myo-D-inositol phosphate synthase was discovered by Bachhawat and Mande in 1999 (reported in Journal of Molecular Biology). The existence of inositol in prokaryotes is not extensive, but the discovery of this enzyme first in Mycobacterium tuberculosis, nucleated activity towards finding its inhibitors.

Structural studies

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1GR0, 1JKF, 1JKI, 1LA2, 1P1F, 1P1H, 1P1I, 1P1J, 1P1K, 1RM0, 1VJP, and 1VKO.

Related Research Articles

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.

<span class="mw-page-title-main">Xylose metabolism</span>

D-Xylose is a five-carbon aldose that can be catabolized or metabolized into useful products by a variety of organisms.

In enzymology, an inositol 1-methyltransferase is an enzyme that catalyzes the chemical reaction

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

The enzyme glycosylphosphatidylinositol diacylglycerol-lyase catalyzes the reaction

<span class="mw-page-title-main">Phosphatidylinositol diacylglycerol-lyase</span>

The enzyme phosphatidylinositol diacylglycerol-lyase catalyzes the following reaction:

<span class="mw-page-title-main">Chorismate synthase</span>

The enzyme chorismate synthase catalyzes the chemical reaction

The enzyme 4-phytase (EC 3.1.3.26) catalyzes the following reaction:

The enzyme glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) is an enzyme that catalyzes the chemical reaction

The enzyme inositol-1,4-bisphosphate 1-phosphatase (EC 3.1.3.57) catalyzes the reaction

<span class="mw-page-title-main">Inositol-phosphate phosphatase</span> Class of enzymes

The enzyme Inositol phosphate-phosphatase is of the phosphodiesterase family of enzymes. It is involved in the phosphophatidylinositol signaling pathway, which affects a wide array of cell functions, including but not limited to, cell growth, apoptosis, secretion, and information processing. Inhibition of inositol monophosphatase may be key in the action of lithium in treating bipolar disorder, specifically manic depression.

The enzyme phosphatidylinositol-3,4-bisphosphate 4-phosphatase (EC 3.1.3.66) that catalyzes the reaction

The enzyme phosphatidylinositol-3-phosphatase (EC 3.1.3.64) catalyzes the reaction

<span class="mw-page-title-main">1-phosphatidylinositol 4-kinase</span> Class of enzymes

In enzymology, a 1-phosphatidylinositol 4-kinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">CDP-diacylglycerol—inositol 3-phosphatidyltransferase</span>

In enzymology, a CDP-diacylglycerol—inositol 3-phosphatidyltransferase is an enzyme that catalyzes the chemical reaction

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

In enzymology, an inositol-tetrakisphosphate 1-kinase is an enzyme that catalyzes the chemical reaction

Bisphosphate may refer to:

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.

<span class="mw-page-title-main">5-Deoxyinositol</span> Chemical compound

5-Deoxyinositol (quercitol) is a cyclitol. It can be found in wines aged in oak wood barrels. It can also be found in Quercus sp. (oaks) and in Gymnema sylvestre. It is different from quercetol, a synonym of quercetin.

References

  1. Klig LS, Zobel PA, Devry CG, Losberger C (June 1994). "Comparison of INO1 gene sequences and products in Candida albicans and Saccharomyces cerevisiae". Yeast. 10 (6): 789–800. doi:10.1002/yea.320100609. PMID   7975896. S2CID   21530024.
  2. Majumder AL, Johnson MD, Henry SA (September 1997). "1L-myo-inositol-1-phosphate synthase". Biochim. Biophys. Acta. 1348 (1–2): 245–56. doi:10.1016/s0005-2760(97)00122-7. PMID   9370339.

Further reading

Bachhawat N and Mande SC (1999) J. Mol. Biol. Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1-phosphate synthase enzyme. 291, 531–536.

This article incorporates text from the public domain Pfam and InterPro: IPR013021