Isocitrate dehydrogenase kinase/phosphatase
Biochimie, ISSN: 0300-9084, Vol: 71, Issue: 9, Page: 1051-1057
1989
- 33Citations
- 25Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations33
- Citation Indexes33
- 33
- CrossRef28
- Captures25
- Readers25
- 25
Article Description
In Escherichia coli, isocitrate dehydrogenase (IDH) is regulated by phosphorylation. This phosphorylation cycle is catalyzed by an unusual, bifunctional protein: IDH kinase/phosphatase. IDH kinase/phosphatase is expressed from a single gene, aceK, and both activities are catalyzed by the same polypeptide. The amino acid sequence of IDH kinase/phosphatase does not exhibit the characteristics which are typical of other protein kinases, although it does contain a consensus ATP binding site. The available evidence suggests that the IDH kinase and IDH phosphatase reactions occur at the same active site and that the IDH phosphatase reaction results from the back reaction of IDH kinase tightly coupled to ATP hydrolysis.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0300908489901107; http://dx.doi.org/10.1016/0300-9084(89)90110-7; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0024453153&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/2557093; https://linkinghub.elsevier.com/retrieve/pii/0300908489901107; http://dx.doi.org/10.1016/0300-9084%2889%2990110-7; https://dx.doi.org/10.1016/0300-9084%2889%2990110-7
Elsevier BV
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