Identification of fungal oxaloacetate hydrolyase within the isocitrate lyase/PEP mutase enzyme superfamily using a sequence marker-based method

2007 ◽  
Vol 70 (1) ◽  
pp. 157-166 ◽  
Author(s):  
Henk-Jan Joosten ◽  
Ying Han ◽  
Weiling Niu ◽  
Jacques Vervoort ◽  
Debra Dunaway-Mariano ◽  
...  
Keyword(s):  
Isocitrate Lyase ◽  
Enzyme Superfamily ◽  
Pep Mutase

Structure and Function of 2,3-Dimethylmalate Lyase, a PEP Mutase/Isocitrate Lyase Superfamily Member

2009 ◽  
Vol 386 (2) ◽  
pp. 486-503 ◽  
Author(s):  
Buvaneswari Narayanan ◽  
Weiling Niu ◽  
Henk-Jan Joosten ◽  
Zhimin Li ◽  
Remko K.P. Kuipers ◽  
...  
Keyword(s):  
Isocitrate Lyase ◽  
Structure And Function ◽  
Pep Mutase ◽  
And Function

Structure and Kinetics of Phosphonopyruvate Hydrolase fromVoriovoraxsp. Pal2:  New Insight into the Divergence of Catalysis within the PEP Mutase/Isocitrate Lyase Superfamily†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (38) ◽  
pp. 11491-11504 ◽  
Author(s):  
Celia C. H. Chen ◽  
Ying Han ◽  
Weiling Niu ◽  
Anna N. Kulakova ◽  
Andrew Howard ◽  
...  
Keyword(s):  
Isocitrate Lyase ◽  
Pep Mutase ◽  
Kinetics Of ◽  
Insight Into

scholarly journals Structure and Function of PA4872 fromPseudomonas aeruginosa, a Novel Class of Oxaloacetate Decarboxylase from the PEP Mutase/Isocitrate Lyase Superfamily†,‡

Biochemistry ◽  
2008 ◽  
Vol 47 (1) ◽  
pp. 167-182 ◽  
Author(s):  
Buvaneswari C. Narayanan ◽  
Weiling Niu ◽  
Ying Han ◽  
Jiwen Zou ◽  
Patrick S. Mariano ◽  
...  
Keyword(s):  
Isocitrate Lyase ◽  
Structure And Function ◽  
Oxaloacetate Decarboxylase ◽  
Pep Mutase ◽  
And Function

Diversity of Function in the Isocitrate Lyase Enzyme Superfamily:  TheDianthus caryophyllusPetal Death Protein Cleaves α-Keto and α-Hydroxycarboxylic Acids†

Biochemistry ◽  
2005 ◽  
Vol 44 (50) ◽  
pp. 16365-16376 ◽  
Author(s):  
Zhibing Lu ◽  
Xiaohua Feng ◽  
Ling Song ◽  
Ying Han ◽  
Alexander Kim ◽  
...  
Keyword(s):  
Isocitrate Lyase ◽  
Hydroxycarboxylic Acids ◽  
Enzyme Superfamily

scholarly journals Stereochemical Course of the Isocitrate Lyase Reaction

1964 ◽  
Vol 239 (12) ◽  
pp. 4268-4271 ◽  
Author(s):  
M. Sprecher ◽  
R. Berger ◽  
D.B. Sprinson
Keyword(s):  
Isocitrate Lyase

Disruption of genes for the enhanced biosynthesis of α-ketoglutarate in Corynebacterium glutamicum

2012 ◽  
Vol 58 (3) ◽  
pp. 278-286 ◽  
Author(s):  
Jae-Hyung Jo ◽  
Hye-Young Seol ◽  
Yun-Bom Lee ◽  
Min-Hong Kim ◽  
Hyung-Hwan Hyun ◽  
...  
Keyword(s):  
Corynebacterium Glutamicum ◽  
Biosynthetic Pathway ◽  
Isocitrate Lyase ◽  
Glutamate Synthase ◽  
Flask Culture ◽  
Control Strain ◽  
Enhanced Production ◽  
Key Enzyme ◽  
Microbial Strains ◽  
Glyoxylate Pathway

The development of microbial strains for the enhanced production of α-ketoglutarate (α-KG) was investigated using a strain of Corynebacterium glutamicum that overproduces of l-glutamate, by disrupting three genes involved in the α-KG biosynthetic pathway. The pathways competing with the biosynthesis of α-KG were blocked by knocking out aceA (encoding isocitrate lyase, ICL), gdh (encoding glutamate dehydrogenase, l-gluDH), and gltB (encoding glutamate synthase or glutamate-2-oxoglutarate aminotransferase, GOGAT). The strain with aceA, gltB, and gdh disrupted showed reduced ICL activity and no GOGAT and l-gluDH activities, resulting in up to 16-fold more α-KG production than the control strain in flask culture. These results suggest that l-gluDH is the key enzyme in the conversion of α-KG to l-glutamate; therefore, prevention of this step could promote α-KG accumulation. The inactivation of ICL leads the carbon flow to α-KG by blocking the glyoxylate pathway. However, the disruption of gltB did not affect the biosynthesis of α-KG. Our results can be applied in the industrial production of α-KG by using C. glutamicum as producer.

scholarly journals Production of succinate by engineered strains of Synechocystis PCC 6803 overexpressing phosphoenolpyruvate carboxylase and a glyoxylate shunt

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Claudia Durall ◽  
Kateryna Kukil ◽  
Jeffrey A. Hawkes ◽  
Alessia Albergati ◽  
Peter Lindblad ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Isocitrate Lyase ◽  
Tricarboxylic Acid Cycle ◽  
Cell Metabolism ◽  
Tca Cycle ◽  
Malate Synthase ◽  
Glyoxylate Shunt ◽  
Control Strain ◽  
Genes Encoding ◽  
Pcc 6803

Abstract Background Cyanobacteria are promising hosts for the production of various industrially important compounds such as succinate. This study focuses on introduction of the glyoxylate shunt, which is naturally present in only a few cyanobacteria, into Synechocystis PCC 6803. In order to test its impact on cell metabolism, engineered strains were evaluated for succinate accumulation under conditions of light, darkness and anoxic darkness. Each condition was complemented by treatments with 2-thenoyltrifluoroacetone, an inhibitor of succinate dehydrogenase enzyme, and acetate, both in nitrogen replete and deplete medium. Results We were able to introduce genes encoding the glyoxylate shunt, aceA and aceB, encoding isocitrate lyase and malate synthase respectively, into a strain of Synechocystis PCC 6803 engineered to overexpress phosphoenolpyruvate carboxylase. Our results show that complete expression of the glyoxylate shunt results in higher extracellular succinate accumulation compared to the wild type control strain after incubation of cells in darkness and anoxic darkness in the presence of nitrate. Addition of the inhibitor 2-thenoyltrifluoroacetone increased succinate titers in all the conditions tested when nitrate was available. Addition of acetate in the presence of the inhibitor further increased the succinate accumulation, resulting in high levels when phosphoenolpyruvate carboxylase was overexpressed, compared to control strain. However, the highest succinate titer was obtained after dark incubation of an engineered strain with a partial glyoxylate shunt overexpressing isocitrate lyase in addition to phosphoenolpyruvate carboxylase, with only 2-thenoyltrifluoroacetone supplementation to the medium. Conclusions Heterologous expression of the glyoxylate shunt with its central link to the tricarboxylic acid cycle (TCA) for acetate assimilation provides insight on the coordination of the carbon metabolism in the cell. Phosphoenolpyruvate carboxylase plays an important role in directing carbon flux towards the TCA cycle.

Co-ordinate regulation of genes involved in storage lipid mobilization in Arabidopsis thaliana

2001 ◽  
Vol 29 (2) ◽  
pp. 283-286 ◽  
Author(s):  
E. L. Rylott ◽  
M. A. Hooks ◽  
I. A. Graham
Keyword(s):  
Arabidopsis Thaliana ◽  
Enzyme Activities ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Molecular Genetic ◽  
Regulation Of Gene Expression ◽  
Growth Period ◽  
Malate Synthase ◽  
The Glyoxylate Cycle

Molecular genetic approaches in the model plant Arabidopsis thaliana (ColO) are shedding new light on the role and control of the pathways associated with the mobilization of lipid reserves during oilseed germination and post-germinative growth. Numerous independent studies have reported on the expression of individual genes encoding enzymes from the three major pathways: β-oxidation, the glyoxylate cycle and gluconeogenesis. However, a single comprehensive study of representative genes and enzymes from the different pathways in a single plant species has not been done. Here we present results from Arabidopsis that demonstrate the co-ordinate regulation of gene expression and enzyme activities for the acyl-CoA oxidase- and 3-ketoacyl-CoA thiolasemediated steps of β-oxidation, the isocitrate lyase and malate synthase steps of the glyoxylate cycle and the phosphoenolpyruvate carboxykinase step of gluconeogenesis. The mRNA abundance and enzyme activities increase to a peak at stage 2, 48 h after the onset of seed germination, and decline thereafter either to undetectable levels (for malate synthase and isocitrate lyase) or low basal levels (for the genes of β-oxidation and gluconeogenesis). The co-ordinate induction of all these genes at the onset of germination raises the possibility that a global regulatory mechanism operates to induce the expression of genes associated with the mobilization of storage reserves during the heterotrophic growth period.

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