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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

GGT1 glutamate:glyoxylate aminotransferase

Identified by cloning the gene that corresponded to a purified protein having glyoxylate aminotransferase activity. Localized to the peroxisome and thought to be involved in photorespiration/ metabolic salvage pathway. (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, GGT4, GGTI
Papers on GGT1
Arabidopsis thaliana ggt1 photorespiratory mutants maintain leaf carbon/nitrogen balance by reducing RuBisCO content and plant growth.
Hodges et al., Orsay, France. In Plant J, Sep 2015
Metabolic and physiological analyses of glutamate:glyoxylate aminotransferase 1 (GGT1) mutants were performed at the global leaf scale to elucidate the mechanisms involved in their photorespiratory growth phenotype.
Hanigan et al., Oklahoma City, United States. In J Biol Chem, Aug 2015
γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
Immunolabeling of gamma-glutamyl transferase 5 in normal human tissues reveals that expression and localization differ from gamma-glutamyl transferase 1.
Wirsig-Wiechmann et al., Oklahoma City, United States. In Histochem Cell Biol, May 2015
GGT5 was expressed in some of the same tissues that have been shown to express gamma-glutamyl transferase (GGT1), the only other enzymatically active protein in this family.
Proteome readjustments in the apoplastic space of Arabidopsis thaliana ggt1 mutant leaves exposed to UV-B radiation.
Masi et al., Padova, Italy. In Front Plant Sci, 2014
In Arabidopsis thaliana, the gamma-glutamyl transferase isoform (GGT1) bound to the cell wall takes part in the so-called gamma-glutamyl cycle for extracellular glutathione degradation and recovery, and may be implicated in redox sensing and balance.
Interactive effects of a common γ-glutamyltransferase 1 variant and low high-density lipoprotein-cholesterol on diabetic macro- and micro-angiopathy.
Ogawa et al., Kumamoto, Japan. In Cardiovasc Diabetol, 2014
Risk factors for a high brachial-ankle pulse wave velocity (baPWV) (≥1750 cm/sec) or diabetic retinopathy (DR) were determined using a generalized estimating equations approach, receiver operating characteristic (ROC) analysis or Cox proportional hazards model, etc. RESULTS: The frequency of the GGT1 G allele was 20.8% in the T2DM subjects, and no associations were found between the GGT1 genotype and risk of T2DM.
Genetics and treatment options for recurrent acute and chronic pancreatitis.
Whitcomb et al., Pittsburgh, United States. In Curr Treat Options Gastroenterol, 2014
New findings of pancreas disease-associated risk variants have been reported in the CPA1, GGT1, CLDN2, MMP1, MTHFR, and other genes.
Identification of metabolic signatures associated with erlotinib resistance of non-small cell lung cancer cells.
Koh et al., Shizuoka, Japan. In Anticancer Res, 2014
Copy number gains in v-myc avian myelocytomatosis viral oncogene homolog (MYC), glutathione-S-transferase theta 2 (GSTT2), gamma-glutamyltransferase 1 (GGT1), and GGT5 were also detected, suggesting that amplification of these genes confers glutamine addiction in PC-9ER cells.
What determines human body odour?
Nakamura et al., Kitakyūshū, Japan. In Exp Dermatol, 2014
Moreover, SG-3MSH was processed to 3M3SH by γ-glutamyl-transferase 1 (GGT1), which was abundantly expressed in apocrine sweat glands.
Glutathione-conjugated sulfanylalkanols are substrates for ABCC11 and γ-glutamyl transferase 1: a potential new pathway for the formation of odorant precursors in the apocrine sweat gland.
Jovanovic et al., Hamburg, Germany. In Exp Dermatol, 2014
Critically, the apocrine sweat gland was demonstrated to express γ-glutamyl transferase 1 (GGT1) protein, which is known to catalyse the deglutamylation of glutathionyl conjugates.
Detection of distinct glycosylation patterns on human γ-glutamyl transpeptidase 1 using antibody-lectin sandwich array (ALSA) technology.
Hanigan et al., In Bmc Biotechnol, 2013
BACKGROUND: γ-Glutamyl transpeptidase 1 (GGT1) is an N-glycosylated membrane protein that catabolizes extracellular glutathione and other γ-glutamyl-containing substrates.
Ubiquinol reduces gamma glutamyltransferase as a marker of oxidative stress in humans.
Döring et al., Kiel, Germany. In Bmc Res Notes, 2013
Serum gamma-glutamyltransferase (GGT) activity is associated with cardiovascular diseases.
Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
Mooers et al., In J Biol Chem, 2013
The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
Identification of the galactosyltransferase of Cryptococcus neoformans involved in the biosynthesis of basidiomycete-type glycosylinositolphosphoceramide.
Aebi et al., Zürich, Switzerland. In Glycobiology, 2013
In this study, we identified and determined the gene structure of the enzyme Ggt1, which catalyzes the transfer of a galactose residue to MIPC.
Targeting protein prenylation for cancer therapy.
Sebti et al., Tampa, United States. In Nat Rev Cancer, 2011
This observation prompted the development of inhibitors of farnesyltransferase (FT) and geranylgeranyl-transferase 1 (GGT1) as potential anticancer drugs.
Altered ABA, proline and hydrogen peroxide in an Arabidopsis glutamate:glyoxylate aminotransferase mutant.
Zhu et al., Riverside, United States. In Plant Mol Biol, 2007
Mutations in GGT1 result in altered abscisic acid sensitivity.
Characterization of the extracellular gamma-glutamyl transpeptidases, GGT1 and GGT2, in Arabidopsis.
Oliver et al., Ames, United States. In Plant J, 2007
These observations suggest that GGT1 is important in preventing oxidative stress by metabolizing extracellular glutathione disulfide, while GGT2 might be important in transporting glutathione into developing seeds.
[Gamma Glutamyltransferase].
Ohkawa et al., In Nihon Rinsho, 1995
Gamma-Glutamyltransferase (GGT), formerly called gamma-glutamyltranspeptidase, is predominantly a membrane-bound enzyme.
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