Induction of glyoxylate cycle enzymes in rat liver upon food starvation

Popov, Vasily N.; Igamberdiev, Abir U.; Schnarrenberger, Claus; Volvenkin, S. V.

doi:10.1016/0014-5793(96)00668-0

Cited by 37 publications

(14 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have shown earlier that the glyoxylate cycle is induced in the liver of starved rats [5, 6]. The properties of purified enzymes isolated from the liver of alloxan‐treated rats corresponded to previously published data for isocitrate lyase isolated from the liver of starved rats.…”

Section: Discussionsupporting

confidence: 83%

See 1 more Smart Citation

Glyoxylate cycle enzymes are present in liver peroxisomes of alloxan‐treated rats

et al. 1998

View full text Add to dashboard Cite

Key enzymes of the glyoxylate cycle, isocitrate lyase (ICL) and malate synthase (MS), have been detected in the liver of alloxan-treated rats. The activity of ICL in rat liver was 0.040 W Wmol/min/mg protein and the activity of MS was 0.022 W Wmol/ min/mg protein. These enzymes were associated with the peroxisomal fraction. The activities of citrate synthase, malate synthase and malate dehydrogenase detected in the peroxisomal fraction were also increased by alloxan treatment. Isocitrate lyase was partially purified and displayed catalytic and regulatory properties similar to those of the enzyme isolated from the liver of starved rats FEBS Lett. 391, 87^90).z 1998 Federation of European Biochemical Societies.

show abstract

Section: Discussionsupporting

confidence: 83%

“…We have determined the activities of these enzymes, purified and characterized them. These data established the existence of these key enzymes of the glyoxylate cycle in mammalian tissue [5, 6]. It has provided the biochemical basis for the physiological phenomena of de novo glycogen synthesis in rat liver upon starvation [7, 8].…”

Section: Introductionmentioning

confidence: 99%

Glyoxylate cycle enzymes are present in liver peroxisomes of alloxan‐treated rats

et al. 1998

View full text Add to dashboard Cite

show abstract

“…Surprisingly, the glyoxylate cycle was also detected in livers of starving rats where it is presumably associated with glycogen formation, a similar situation to carbohydrate synthesis in bacteria or plants (Popov et al 1996). Among bacteria, studies have been performed in Escherichia coli where elevated levels of the glyoxylate cycle enzymes were detected (Maloy et al 1980).…”

mentioning

confidence: 92%

Molecular cloning, heterologous expression, and functional characterisation of a malate synthase gene fromStreptomyces coelicolorA3(2)

Loke¹,

Sim²

2000

Can. J. Microbiol.

View full text Add to dashboard Cite

With the rapid generation of genetic information from the Streptomyces coelicolor genome project, deciphering the relevant gene products is critical for understanding the genetics of this model streptomycete. A putative malate synthase gene (aceB) from S. coelicolor A3(2) was identified by homology-based analysis, cloned by polymerase chain reaction, and fully sequenced on both strands. The putative malate synthase from S. coelicolor has an amino acid identity of 77% with the malate synthase of S. clavuligerus, and possesses an open reading frame which codes for a protein of 540 amino acids. In order to establish the identity of this gene, the putative aceB clones were subcloned into the expression vector pET24a, and heterologously expressed in Escherichia coli BL21(DE3). Soluble cell-free extracts containing the recombinant putative malate synthase exhibited a specific activity of 1623 (nmol.mg-1.min-1), which is an increment of 92-fold compared to the non-recombinant control. Thus, the gene product was confirmed to be a malate synthase. Interestingly, the specific activity of S. coelicolor malate synthase was found to be almost 8-fold higher than the specific activity of S. clavuligerus malate synthase under similar expression conditions. Furthermore, the genomic organisation of the three Streptomyces aceB genes cloned thus far is different from that of other bacterial malate synthases, and warrants further investigation.

show abstract

“…The gloxylate cycle, which was first proposed by Kornberg and Krebs [1,2] in bacteria growing on acetate [3], is an anaplerotic metabolic pathway which plays an important role in the biogenesis of carbohydrates from C2 compounds [4,5].There are alternative pathways to the glyoxylate cycle in some bacteria [6][7][8].This pathway is widespread in living organisms (Bacteria, Eukarya and Archaea), and the two key enzymes (isocitrate lyase and malate synthase) have been detected in various eubacteria, fungi, plants and even some animals [4,6].…”

Section: Introductionmentioning

confidence: 99%

Relationship between Glyoxylate Cycle and Nitrification Efficiency based on Heterotrophic Nitrification Bacterium Acinetobacter sp.Y1

Li¹,

Liu²

2017

Proceedings of the 2nd 2016 International Conference on Sustainable Development (ICSD 2016)

View full text Add to dashboard Cite

Abstract-The growth and ammonium removal ability of heterotrophic nitrification bacterium are strongly influenced by carbon sources, as well as the activities of key enzymes of glyoxylate cycle. To obtain a better insight into the relationship between glyoxylate cycle and nitrification, the two key enzymes of glyoxylate cycle and the ammonium removal ability of Acinetobacter sp.Y1 grew with different carbon sources were examined. Strain Y1 showed a wide organic carbon substrates, and grew but no nitrify in the medium with sucrose and glycerol as sole carbon source. The strain Y1 showed the most activities of isocitrate lyase and malate synthase when the ammonium removal rate reached highest, and no activities of the two enzymes were detected when the strain grew without nitrification phase. The positive correlation relationship was found between the glyoxylate cycle and nitrification.

show abstract

Induction of glyoxylate cycle enzymes in rat liver upon food starvation

Cited by 37 publications

References 16 publications

Glyoxylate cycle enzymes are present in liver peroxisomes of alloxan‐treated rats

Glyoxylate cycle enzymes are present in liver peroxisomes of alloxan‐treated rats

Molecular cloning, heterologous expression, and functional characterisation of a malate synthase gene fromStreptomyces coelicolorA3(2)

Relationship between Glyoxylate Cycle and Nitrification Efficiency based on Heterotrophic Nitrification Bacterium Acinetobacter sp.Y1

Contact Info

Product

Resources

About