Gene Association: GSX1
UniProt Search:
GSX1 (PROTEIN_CODING)
Function Description: GS homeobox 1
found 10 associated metabolites with current gene based on the text mining result from the pubmed database.
Oxidized glutathione
Oxidized glutathione, also known as glutathione disulfide or GSSG, belongs to the class of organic compounds known as peptides. Peptides are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by the formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another. In humans, oxidized glutathione is involved in the metabolic disorder called leukotriene C4 synthesis deficiency pathway. Outside of the human body, oxidized glutathione has been detected, but not quantified in several different foods, such as leeks, star anises, mamey sapotes, climbing beans, and common persimmons. Oxidized glutathione is a glutathione dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized. Glutathione participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidase. It is also important as a hydrophilic molecule that is added to lipophilic toxins and waste in the liver during biotransformation before they can become part of the bile. Glutathione is also needed for the detoxification of methylglyoxal, a toxin produced as a by-product of metabolism. This detoxification reaction is carried out by the glyoxalase system. Glyoxalase I (EC 4.4.1.5) catalyzes the conversion of methylglyoxal and reduced glutathione into S-D-lactoyl-glutathione. Glyoxalase II (EC 3.1.2.6) catalyzes the hydrolysis of S-D-lactoyl-glutathione into glutathione and D-lactate. Glutathione disulfide (GSSG) - oxidized glutathione - is a disulfide derived from two glutathione molecules. In living cells, glutathione disulfide is reduced into two molecules of glutathione with reducing equivalents from the coenzyme NADPH. This reaction is catalyzed by the enzyme glutathione reductase. [Wikipedia]. Glutathione disulfide is found in many foods, some of which are jute, millet, malabar plum, and acorn. [Spectral] Glutathione disulfide (exact mass = 612.15196) and 3,4-Dihydroxy-L-phenylalanine (exact mass = 197.06881) and AMP (exact mass = 347.06308) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] Glutathione disulfide (exact mass = 612.15196) and AMP (exact mass = 347.06308) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Acquisition and generation of the data is financially supported in part by CREST/JST. KEIO_ID G008; [MS2] KO008986 C26170 - Protective Agent KEIO_ID G008 Glutathione oxidized (L-Glutathione oxidized) is produced by the oxidation of glutathione. Detoxification of reactive oxygen species is accompanied by production of glutathione oxidized. Glutathione oxidized can be used for the research of sickle cells and erythrocytes[1][2]. Glutathione oxidized (GSSG) is produced by the oxidation of glutathione. Detoxification of reactive oxygen species is accompanied by production of glutathione oxidized. Glutathione oxidized can be used for the research of sickle cells and erythrocytes[1].
gamma-Glutamylcysteine
gamma-Glutamylcysteine is a dipeptide composed of gamma-glutamate and cysteine, and is a proteolytic breakdown product of larger proteins. It belongs to the family of N-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid which bears an acyl group at its terminal nitrogen atom. gamma-Glutamylcysteine is an incomplete breakdown product of protein digestion or protein catabolism. Some dipeptides are known to have physiological or cell-signaling effects although most are simply short-lived intermediates on their way to specific amino acid degradation pathways following further proteolysis. gamma-Glutamylcysteine is a product of enzyme glutamate-cysteine ligase [EC 6.3.2.2] and a substrate of enzyme glutathione synthase [EC 6.3.2.3] in the glutamate metabolism pathway (KEGG). G-Glutamylcysteine is a product of enzyme glutamate-cysteine ligase [EC 6.3.2.2] and a substrate of enzyme glutathione synthase [EC 6.3.2.3] in glutamate metabolism pathway (KEGG). gamma-Glutamyl-cysteine is found in many foods, some of which are cardamom, hyacinth bean, oil palm, and pak choy. Acquisition and generation of the data is financially supported in part by CREST/JST. Gamma-glutamylcysteine (γ-Glutamylcysteine), a dipeptide containing cysteine and glutamic acid, is a precursor to glutathione (GSH). Gamma-glutamylcysteine is a cofactor for glutathione peroxidase (GPx) to increase GSH levels[1].
5-Hydroxymethyl-2-furancarboxaldehyde
5-hydroxymethylfurfural is a member of the class of furans that is furan which is substituted at positions 2 and 5 by formyl and hydroxymethyl substituents, respectively. Virtually absent from fresh foods, it is naturally generated in sugar-containing foods during storage, and especially by drying or cooking. It is the causative component in honey that affects the presystemic metabolism and pharmacokinetics of GZ in-vivo. It has a role as an indicator and a Maillard reaction product. It is a member of furans, an arenecarbaldehyde and a primary alcohol. Aes-103 has been used in trials studying the treatment and prevention of Hypoxia, Anemia, Sickle Cell, and Sickle Cell Disease. 5-Hydroxymethylfurfural is a natural product found in Prunus mume, Tussilago farfara, and other organisms with data available. 5-Hydroxymethyl-2-furancarboxaldehyde belongs to the family of Furans. These are compounds containing a furan ring, which is a five-member aromatic ring with one oxygen atom, four carbon atoms. 5-Hydroxymethyl-2-furancarboxaldehyde is found in garden onion. Obtainable from various carbohydrates. 5-Hydroxymethyl-2-furancarboxaldehyde is present in tomatoes, tobacco oil etc. 5-Hydroxymethyl-2-furancarboxaldehyde is a constituent of numerous plant species. 5-Hydroxymethyl-2-furancarboxaldehyde is used as an index of heat treatment and deterioration in food such as tomato paste, honey and fruit juices. Also an indicator of adulteration with acid-converted invert sugars. 5-Hydroxymethylfurfural is a biomarker for the consumption of beer 5-Hydroxymethyl-2-furancarboxaldehyde or simply HMF is obtainable from various carbohydrates. It is found in garden tomatoes, garden onion, and tobacco oil. Constituent of numerous plant spp.. Used as an index of heat treatment and deterioration in food such as tomato paste, honey and fruit juices. Also an indicator of adulteration with acid-converted invert sugars. 5-Hydroxymethylfurfural is a biomarker for the consumption of beer. 5-Hydroxymethylfurfural (2-Hydroxymethyl-5-furfural), derived from Cornus officinalis, inhibits yeast growth and fermentation as stressors. 5-Hydroxymethylfurfural (2-Hydroxymethyl-5-furfural), derived from Cornus officinalis, inhibits yeast growth and fermentation as stressors.
Gamma-glutamylcysteine
MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; RITKHVBHSGLULN_STSL_0116_5-Glutamylcysteine_8000fmol_180506_S2_LC02_MS02_219; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I. Gamma-glutamylcysteine (γ-Glutamylcysteine), a dipeptide containing cysteine and glutamic acid, is a precursor to glutathione (GSH). Gamma-glutamylcysteine is a cofactor for glutathione peroxidase (GPx) to increase GSH levels[1].
67-47-0
5-Hydroxymethylfurfural (2-Hydroxymethyl-5-furfural), derived from Cornus officinalis, inhibits yeast growth and fermentation as stressors. 5-Hydroxymethylfurfural (2-Hydroxymethyl-5-furfural), derived from Cornus officinalis, inhibits yeast growth and fermentation as stressors.
Oxiglutatione
C26170 - Protective Agent Glutathione oxidized (L-Glutathione oxidized) is produced by the oxidation of glutathione. Detoxification of reactive oxygen species is accompanied by production of glutathione oxidized. Glutathione oxidized can be used for the research of sickle cells and erythrocytes[1][2]. Glutathione oxidized (GSSG) is produced by the oxidation of glutathione. Detoxification of reactive oxygen species is accompanied by production of glutathione oxidized. Glutathione oxidized can be used for the research of sickle cells and erythrocytes[1].
