Results 11 to 20 of about 6,068 (228)
Multi-level kinetic model explaining diverse roles of isozymes in prokaryotes. [PDF]
PLoS ONE, 2014 Current standard methods for kinetic and genomic modeling cannot provide deep insight into metabolic regulation. Here, we developed and evaluated a multi-scale kinetic modeling approach applicable to any prokaryote. Specifically, we highlight the primary
Jiri Jablonsky +2 more
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Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis
Molecules, 2021 Lactobacillus sp. have long been studied for their great potential in probiotic applications. Recently, proteomics analysis has become a useful tool for studies on potential lactobacilli probiotics.
Bernadette B. Bagon +4 more
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A hypothesis for the evolution of nuclear-encoded, plastid-targeted glyceraldehyde-3-phosphate dehydrogenase genes in "chromalveolate" members. [PDF]
PLoS ONE, 2009 Eukaryotes bearing red alga-derived plastids--photosynthetic alveolates (dinoflagellates plus the apicomplexan Toxoplasma gondii plus the chromerid Chromera velia), photosynthetic stramenopiles, haptophytes, and cryptophytes--possess unique plastid ...
Kiyotaka Takishita +3 more
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Halophyte Nitraria billardieri CIPK25 promotes photosynthesis in Arabidopsis under salt stress
Frontiers in Plant Science, 2022 The calcineurin B-like (CBL)-interacting protein kinases (CIPKs), a type of plant-specific genes in the calcium signaling pathway, function in response to adverse environments.
Lu Lu +9 more
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Glyceraldehyde‐3‐phosphate activates auto‐ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase [PDF]
FEBS Letters, 1993 Nitric oxide was recently demonstrated to stimulate ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH). Our studies on the effect of glyceraldehyde‐3‐phosphate (GA3P), the natural substrate of dehydrogenase activity of GAPDH, indicated GA3P to be another very potent activator of ADP‐ribosylation of the enzyme.
Kots, Alexander Ya. +3 more
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Mechanism of glyceraldehyde‐3‐phosphate transfer from aldolase to glyceraldehyde‐3‐phosphate dehydrogenase [PDF]
European Journal of Biochemistry, 1988 The catalytic interaction of glyceraldehyde‐3‐phosphate dehydrogenase with glyceraldehydes‐3‐phosphate has been examined by transient‐state kinetic methods. The results confirm previous reports that the apparent Km for oxidative phosphorylation of glyceraldehydes‐3‐phosphate decreases at least 50‐fold when the substrate is generated in a coupled ...
Kvassman, Jan +2 more
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Microbial Cell Factories, 2020 Background Saccharomyces cerevisiae is being exploited as a cell factory to produce fatty acids and their derivatives as biofuels. Previous studies found that both precursor supply and fatty acid metabolism deregulation are essential for enhanced fatty ...
Yiming Zhang +4 more
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PLoS ONE, 2012 Glyceraldehyde 3-phosphate dehydrogenases (GAPDH) are cytoplasmic glycolytic enzymes that, despite lacking identifiable secretion signals, have been detected at the surface of several prokaryotic and eukaryotic organisms where they exhibit non-glycolytic
Liliana Oliveira +8 more
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Frontiers in Microbiology, 2020 Bacillus cereus 0-9, a Gram-positive endospore-forming bacterium isolated from healthy wheat roots, has biological control capacity against several soil-borne plant diseases of wheat such as sharp eyespot and take-all.
Juanmei Zhang +9 more
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Stimulation of glyceraldehyde‐3‐phosphate dehydrogenase by oxyhemoglobin
FEBS Letters, 1997 Glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme regulated by many diverse mechanisms. In this study we present evidence that GAPDH activity is stimulated in the presence of oxyhemoglobin (2.3‐fold, P<0.005). No stimulation was seen by myoglobin, and only slight stimulation (1.2‐fold, not significant) by methemoglobin was ...
Brookes, Paul S. +3 more
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