Glutathione hydrolase

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Glutathione hydrolase
Identifiers
EC no. 3.4.19.13
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Glutathione hydrolase (EC 3.4.19.13, glutathionase, GGT, gamma-glutamyltranspeptidase) is an enzyme. [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

glutathione + H2O L-cysteinylglycine + L-glutamate

This protein also acts as enzyme EC 2.3.2.2 (gamma-glutamyltransferase).

Related Research Articles

<span class="mw-page-title-main">Gamma-glutamyltransferase</span> Class of enzymes

Gamma-glutamyltransferase is a transferase that catalyzes the transfer of gamma-glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid, a peptide or water. GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione as well as drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a pro-oxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. This transferase is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker.

<span class="mw-page-title-main">Transglutaminase</span> Class of enzymes capable of forming isopeptide bonds in certain regions of proteins

Transglutaminases are enzymes that in nature primarily catalyze the formation of an isopeptide bond between γ-carboxamide groups ( -(C=O)NH2 ) of glutamine residue side chains and the ε-amino groups ( -NH2 ) of lysine residue side chains with subsequent release of ammonia ( NH3 ). Lysine and glutamine residues must be bound to a peptide or a protein so that this cross-linking (between separate molecules) or intramolecular (within the same molecule) reaction can happen. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). The reaction is

Cysteine metabolism refers to the biological pathways that consume or create cysteine. The pathways of different amino acids and other metabolites interweave and overlap to creating complex systems.

<span class="mw-page-title-main">Glutathione synthetase</span> Enzyme

Glutathione synthetase (GSS) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione. Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants.

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

Azaserine is a naturally occurring serine derivative diazo compound with antineoplastic and antibiotic properties deriving from its action as a purinergic antagonist and structural similarity to glutamine. Azaserine acts by competitively inhibiting glutamine amidotransferase, a key enzyme responsible for glutamine metabolism.

Glutamate–cysteine ligase (GCL) EC 6.3.2.2), previously known as γ-glutamylcysteine synthetase (GCS), is the first enzyme of the cellular glutathione (GSH) biosynthetic pathway that catalyzes the chemical reaction:

In enzymology, a glutamate-putrescine ligase is an enzyme that catalyzes the chemical reaction

In enzymology, a glutathionylspermidine synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a gamma-glutamyl-gamma-aminobutyrate hydrolase (EC 3.5.1.94) is an enzyme that catalyzes the chemical reaction

In enzymology, a glutathionylspermidine amidase (EC 3.5.1.78) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Glutathione S-transferase, C-terminal domain</span>

Glutathione S-transferase, C-terminal domain is a structural domain of glutathione S-transferase (GST).

<span class="mw-page-title-main">Gamma-glutamyltransferase 1</span> Protein-coding gene in the species Homo sapiens

Gamma-glutamyltransferase 1 (GGT1), also known as CD224, is a human gene.

<span class="mw-page-title-main">PPP4R1</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 4 regulatory subunit 1 is an enzyme that in humans is encoded by the PPP4R1 gene.

<span class="mw-page-title-main">Gamma-glutamyltransferase 7</span> Protein-coding gene in the species Homo sapiens

Gamma-glutamyltransferase 7 is an enzyme that in humans is encoded by the GGT7 gene.

<span class="mw-page-title-main">Gamma-glutamyltransferase 5</span> Protein-coding gene in the species Homo sapiens

Gamma-glutamyltransferase 5 is an enzyme that in humans is encoded by the GGT5 gene.

4-(γ-Glutamylamino)butanoic acid is molecule that consists of L-glutamate conjugated to γ-aminobutyric acid (GABA). It is the substrate of the enzyme γ-glutamyl-γ-aminobutyrate hydrolase, which is involved in the biosynthesis of polyamines.

<span class="mw-page-title-main">Neutral cholesterol ester hydrolase 1</span> Protein-coding gene in the species Homo sapiens

Neutral cholesterol ester hydrolase 1 (NCEH) also known as arylacetamide deacetylase-like 1 (AADACL1) or KIAA1363 is an enzyme that in humans is encoded by the NCEH1 gene.

Endo-α-N-acetylgalactosaminidase (EC 3.2.1.97, endo-α-acetylgalactosaminidase, endo-α-N-acetyl-D-galactosaminidase, mucinaminylserine mucinaminidase, D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase, endo-α-GalNAc-ase, D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase) is an enzyme with systematic name glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Gamma-glutamyl hydrolase</span> Protein-coding gene in the species Homo sapiens

Ghk.

Leukotriene-C4 hydrolase (EC 3.4.19.14, gamma-glutamyl leukotrienase) is an enzyme. Gamma-glutamyltransferase 5 (GGT5) is a human gene which encodes an enzyme protein that belongs to this class of enzymes. This enzyme catalyses the following chemical reaction

References

  1. Hanigan MH, Ricketts WA (June 1993). "Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase". Biochemistry. 32 (24): 6302–6. doi:10.1021/bi00075a026. PMID   8099811.
  2. Suzuki H, Kumagai H (November 2002). "Autocatalytic processing of gamma-glutamyltranspeptidase". The Journal of Biological Chemistry. 277 (45): 43536–43. doi: 10.1074/jbc.m207680200 . PMID   12207027.
  3. Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K (April 2006). "Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate". Proceedings of the National Academy of Sciences of the United States of America. 103 (17): 6471–6. Bibcode:2006PNAS..103.6471O. doi: 10.1073/pnas.0511020103 . PMC   1458908 . PMID   16618936.
  4. Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ (January 2007). "Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad". The Journal of Biological Chemistry. 282 (1): 534–41. doi: 10.1074/jbc.m607694200 . PMID   17107958.
  5. Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K (January 2007). "Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism". The Journal of Biological Chemistry. 282 (4): 2433–9. doi: 10.1074/jbc.m607490200 . PMID   17135273.
  6. Wickham S, West MB, Cook PF, Hanigan MH (July 2011). "Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes". Analytical Biochemistry. 414 (2): 208–14. doi:10.1016/j.ab.2011.03.026. PMC   3099546 . PMID   21447318.
  7. Carter BZ, Wiseman AL, Orkiszewski R, Ballard KD, Ou CN, Lieberman MW (May 1997). "Metabolism of leukotriene C4 in gamma-glutamyl transpeptidase-deficient mice". The Journal of Biological Chemistry. 272 (19): 12305–10. doi: 10.1074/jbc.272.19.12305 . PMID   9139674.