The unicellular cyanobacterium Synechocystis sp. PCC 6803 presents a hexameric NAD-specific glutamate dehydrogenase with a molecular mass of 295 kDa. The enzyme differs from the NADP-glutamate dehydrogenase found in the same strain and is coded by a different gene. NAD-glutamate dehydrogenase shows a high coenzyme specificity, catalyzes preferentially glutamate formation and presents Km values for ammonium, NADH and 2-oxoglutarate of 4.5 mM, 50 microM and 1.8 mM respectively. An animating role for the enzyme is discussed.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/0014-5793(91)80719-j | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.
Proc Natl Acad Sci U S A
September 2022
Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Bacterial hibernating 100S ribosomes (the 70S dimers) are excluded from translation and are protected from ribonucleolytic degradation, thereby promoting long-term viability and increased regrowth. No extraribosomal target of any hibernation factor has been reported. Here, we discovered a previously unrecognized binding partner (YwlG) of hibernation-promoting factor (HPF) in the human pathogen .
View Article and Find Full Text PDFAnalysis of Differentially Expressed Genes of Chrysoperla sinica Related to Flight Capacity by Transcriptome.
J Insect Sci
January 2021
College of Plant Protection, Shanxi Agricultural University, Taiyuan, P.R. China.
The lacewing Chrysoperla sinica (Tjeder) is a common natural enemy of many insect pests in China and is frequently employed for biological control programs. Adults make migratory flights after emergence, which reduces their effectiveness as biological control agents. Previously, we proved that 2-d-old unmated females exhibited significantly stronger flight ability than 3-d-old ones.
View Article and Find Full Text PDFStructural Studies of Glutamate Dehydrogenase (Isoform 1) From , an Important Enzyme at the Branch-Point Between Carbon and Nitrogen Metabolism.
Front Plant Sci
June 2020
Center for Biocrystallographic Research Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznań, Poland.
Glutamate dehydrogenase (GDH) releases ammonia in a reversible NAD(P)-dependent oxidative deamination of glutamate that yields 2-oxoglutarate (2OG). In current perception, GDH contributes to Glu homeostasis and plays a significant role at the junction of carbon and nitrogen assimilation pathways. GDHs are members of a superfamily of ELFV (Glu/Leu/Phe/Val) amino acid dehydrogenases and are subdivided into three subclasses, based on coenzyme specificity: NAD-specific, NAD/NADP dual-specific, and NADP-specific.
View Article and Find Full Text PDFImprovement of l-Leucine Production in by Altering the Redox Flux.
Int J Mol Sci
April 2019
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
The production of l-leucine was improved by the disruption of encoding transcriptional regulator and overexpression of the key genes () of the l-leucine biosynthesis pathway in XQ-9. In order to improve l-leucine production, we rationally engineered to enhance l-leucine production, by improving the redox flux. On the basis of this, we manipulated the redox state of the cells by mutating the coenzyme-binding domains of acetohydroxyacid isomeroreductase encoded by , inserting NAD-specific leucine dehydrogenase, encoded by from , and glutamate dehydrogenase encoded by from , instead of endogenous branched-chain amino acid transaminase and glutamate dehydrogenase, respectively.
View Article and Find Full Text PDFFilamentous invasive growth of mutants of the genes encoding ammonia-metabolizing enzymes in the fission yeast Schizosaccharomyces pombe.
PLoS One
November 2017
Department of Bioscience in Daily Life, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan.
The fission yeast Schizosaccharomyces pombe undergoes a switch from yeast to filamentous invasive growth in response to certain environmental stimuli. Among them is ammonium limitation. Amt1, one of the three ammonium transporters in this yeast, is required for the ammonium limitation-induced morphological transition; however, the underlying molecular mechanism remains to be understood.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!