Most micro-organisms contain an NADP-dependent isocitrate dehydrogenase (ICDH) activity. During growth of micro-organisms on acetate as the sole carbon source the two enzymes of the glyoxylate bypass, isocitrate lyase (ICL) and malate synthase (MS), are induced. These two enzymes are required to generate the intermediates of the TCA cycle that are used for biosynthesis. Under these conditions there is competition between the TCA cycle enzyme ICDH and the glyoxylate bypass enzyme ICL for available isocitrate. In E. coli this competition is overcome by the partial phosphorylation and inactivation of ICDH. This mechanism of control has been observed in other enteric bacteria
1. Isoenzymes of NADP-linked isocitrate dehydrogenase, termed IDH-I and IDH-II have been shown to ex...
During growth of Escherichia coli on acetate, the glyoxylate bypass supplies the precursors needed f...
Isocitrate dehydrogenase from Escherichia coli is regulated by a reversible phosphorylation mechanis...
Most micro-organisms contain an NADP-dependent isocitrate dehydrogenase (ICDH) activity. During grow...
The level of activity of the NADP-dependent isocitrate dehydrogenase (ICDH) of E. coli ML308 is cont...
The glyoxylate bypass allows E. coli to generate precursors for biosynthesis during growth on acetat...
As part of an effort to increase our understanding of central metabolic pathways in streptomycetes, ...
During aerobic growth of Escherichia coli on acetate as sole source of carbon and energy, the organi...
During growth of Escherichia coli on acetate, isocitrate dehydrogenase (ICDH) is partially inactivat...
AbstractIsocitrate dehydrogenase from Escherichia coli is regulated by a reversible phosphorylation ...
1. The glyoxylate bypass allows Escherichia coli to generate precursors for biosynthesis during grow...
In this research project, structural aspects of monomeric NADP+-dependent isocitrate dehydrogenase f...
Isocitrate deyhdrogenase (IDH) is a reversible enzyme in the tricarboxylic acid cycle that catalyzes...
Over the last several decades, biochemical research has helped elucidate the structural and function...
In micro-organisms growing on acetate, isocitrate can be metabolized either by the tricarboxylic aci...
1. Isoenzymes of NADP-linked isocitrate dehydrogenase, termed IDH-I and IDH-II have been shown to ex...
During growth of Escherichia coli on acetate, the glyoxylate bypass supplies the precursors needed f...
Isocitrate dehydrogenase from Escherichia coli is regulated by a reversible phosphorylation mechanis...
Most micro-organisms contain an NADP-dependent isocitrate dehydrogenase (ICDH) activity. During grow...
The level of activity of the NADP-dependent isocitrate dehydrogenase (ICDH) of E. coli ML308 is cont...
The glyoxylate bypass allows E. coli to generate precursors for biosynthesis during growth on acetat...
As part of an effort to increase our understanding of central metabolic pathways in streptomycetes, ...
During aerobic growth of Escherichia coli on acetate as sole source of carbon and energy, the organi...
During growth of Escherichia coli on acetate, isocitrate dehydrogenase (ICDH) is partially inactivat...
AbstractIsocitrate dehydrogenase from Escherichia coli is regulated by a reversible phosphorylation ...
1. The glyoxylate bypass allows Escherichia coli to generate precursors for biosynthesis during grow...
In this research project, structural aspects of monomeric NADP+-dependent isocitrate dehydrogenase f...
Isocitrate deyhdrogenase (IDH) is a reversible enzyme in the tricarboxylic acid cycle that catalyzes...
Over the last several decades, biochemical research has helped elucidate the structural and function...
In micro-organisms growing on acetate, isocitrate can be metabolized either by the tricarboxylic aci...
1. Isoenzymes of NADP-linked isocitrate dehydrogenase, termed IDH-I and IDH-II have been shown to ex...
During growth of Escherichia coli on acetate, the glyoxylate bypass supplies the precursors needed f...
Isocitrate dehydrogenase from Escherichia coli is regulated by a reversible phosphorylation mechanis...