ArticleThe Biochemical journal2004
New role for leucyl aminopeptidase in glutathione turnover.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 68 citations in OpenAlex.
- tRF-21LeuTAA Promotes Oxidative Stress by Altering Glutathione Metabolic Enzymes to Support Prostate Cancer Progression.Cancer research · 2025Article
- Development of a Human Preclinical Platform for the Identification of Neuroprotective Compounds.The European journal of neuroscience · 2025Article
- Identification of a staphylococcal dipeptidase involved in the production of human body odor.The Journal of biological chemistry · 2024Article
- Characterization of leucine aminopeptidase (LAP) activity in sweet pepper fruits during ripening and its inhibition by nitration and reducing events.Plant cell reports · 2024Article
- An unexpected role for leucyl aminopeptidase in UV tolerance revealed by a genome-wide fitness assessment in a model cyanobacterium.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Phosphinotripeptidic Inhibitors of Leucylaminopeptidases.International journal of molecular sciences · 2021Article
- Article
- Fruit ripening-associated leucylaminopeptidase with cysteinylglycine dipeptidase activity from durian suggests its involvement in glutathione recycling.BMC plant biology · 2021Article
- Identification and Quantification of Novel Major Metabolites of the Steroidal Aromatase Inhibitor, Exemestane.Drug metabolism and disposition: the biological fate of chemicals · 2018Article
- Article
- A leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei.PLoS pathogens · 2017Article
- Effects on pig immunophysiology, PBMC proteome and brain neurotransmitters caused by group mixing stress and human-animal relationship.PloS one · 2017Article
- Experimental colitis and malnutrition differentially affect the metabolism of glutathione and related sulfhydryl metabolites in different tissues.European journal of nutrition · 2016Article
- Cytological and Proteomic Analyses of Osmunda cinnamomea Germinating Spores Reveal Characteristics of Fern Spore Germination and Rhizoid Tip Growth.Molecular & cellular proteomics : MCP · 2015Article
- Biophysical characterization of a recombinant aminopeptidase II from the thermophilic bacterium Bacillus stearothermophilus.Journal of biological physics · 2014Article
- The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucine.Biological chemistry · 2013Article
- Glutathione degradation by the alternative pathway (DUG pathway) in Saccharomyces cerevisiae is initiated by (Dug2p-Dug3p)2 complex, a novel glutamine amidotransferase (GATase) enzyme acting on glutathione.The Journal of biological chemistry · 2012Article
- Identification of an aminopeptidase from the skeletal muscle of grass carp (Ctenopharyngodon idellus).Fish physiology and biochemistry · 2010Article
- Cysteinyl-glycine in the control of glutathione homeostasis in bovine lenses.Molecular vision · 2010Article
- Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A manganese-dependent cysteinyl-glycine hydrolysing activity has been purified to electrophoretic homogeneity from bovine lens. The characterization of the purified enzyme (molecular mass of the native protein, molecular mass of the subunit and extensive primary structure analysis) allowed the unequivocal attribution of the cysteinyl-glycine hydrolysing activity, which is usually associated with alanyl aminopeptidase (EC 3.4.11.2) or membrane-bound dipeptidase (EC 3.4.13.19), to LAP (leucyl aminopeptidase; EC 3.4.11.1). Analysis of the pH dependence of Cys-Gly hydrolysis catalysed by LAP, supported by a molecular modelling approach to the enzyme-substrate conformation, gave insights into the ability of the enzyme to recognize Cys-Gly as a substrate. Due to the effectiveness of LAP in hydrolysing Cys-Gly (K(m)=0.57 mM, kcat=6.0x10(3) min(-1) at pH 7.4 and 25 degrees C) with respect to other dipeptide substrates, a new role for this enzyme in glutathione turnover is proposed.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.