ArticleThe Biochemical journal1997
Molecular cloning and characterization of the thiolesterase glyoxalase II from Arabidopsis thaliana.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 46 citations in OpenAlex.
- Glyoxalase 2: Towards a Broader View of the Second Player of the Glyoxalase System.Antioxidants (Basel, Switzerland) · 2022Review
- GLYI and D-LDH play key role in methylglyoxal detoxification and abiotic stress tolerance.Scientific reports · 2018Article
- Arabidopsis thaliana glyoxalase 2-1 is required during abiotic stress but is not essential under normal plant growth.PloS one · 2014Article
- Enhancing salt tolerance in a crop plant by overexpression of glyoxalase II.Transgenic research · 2008Article
- Characterization of the gene encoding glyoxalase II from Leishmania donovani: a potential target for anti-parasite drugs.The Biochemical journal · 2006Article
- Structural studies on a mitochondrial glyoxalase II.The Journal of biological chemistry · 2005Article
- The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-beta-lactamase family.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2004Article
- Diverse range of gene activity during Arabidopsis thaliana leaf senescence includes pathogen-independent induction of defense-related genes.Plant molecular biology · 1999Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
cDNA encoding glyoxalase II from Arabidopsis thaliana has been cloned and sequenced. The isolated 894 bp segment included a sequence of 774 bp encoding a protein with a calculated molecular mass of 28,791 Da. The amino acid sequence deduced from the A. thaliana cDNA showed 54% identity with that of the human enzyme. Searches in databanks identified seven additional DNA sequences from different species with high similarity to glyoxalase II. Certain limited regions, one rich in histidine residues, shared 100% identity. A 29 kDa protein with an isoelectric point of 6.2 was obtained by heterologous expression of the A. thaliana cDNA in Escherichia coli. Homogeneous enzyme was obtained by affinity purification and its catalytic parameters with thiolesters of glutathione were similar to those for human glyoxalase II. The structural and functional similarities between glyoxalase II from A. thaliana and from human tissues suggest a common evolutionary origin.
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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.