Escherichia coli isocitrate lyase: properties and comparisons

Hoyt, Jeffrey C.; Robertson, Eugene F.; Berlyn, Kathleen A.; Reeves, Henry C.

doi:10.1016/0304-4165(88)90125-0

Cited by 19 publications

(13 citation statements)

References 30 publications

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“…This product inhibition pattern suggests an ordered uni-bi kinetic mechanism similar to that of the E. coli enzyme (16) the compound became a better inhibitor (53 versus 84% at a 10 mM concentration). The same effect was seen with the E. coli ICL (15). The other compounds examined, malonate, glycolate, and tartrate, gave 33 to 50% inhibition at a 10 mM concentration.…”

Section: Discussionsupporting

confidence: 59%

“…The other compounds examined, malonate, glycolate, and tartrate, gave 33 to 50% inhibition at a 10 mM concentration. The metal cation requirement for Acinetobacter ICL was quite different from that of the E. coli enzyme (15). While magnesium supports maximal activity in both organisms, several other cations exhibit differential behavior.…”

Section: Discussionmentioning

confidence: 83%

“…However, they apparently bind to ICL in a nonproductive manner and are able to inhibit ICL in the presence of magnesium. The E. coli enzyme is inhibited by calcium ion (15), while the P. indigofera enzyme is only slightly affected (36). Surprisingly, ICL from the eukaryote Pinus pinea is significantly inhibited only by beryllium ion (25).…”

Section: Discussionmentioning

confidence: 97%

“…While magnesium supports maximal activity in both organisms, several other cations exhibit differential behavior. In E. coli, manganese(II) supports the ICL reaction at 54% of the magnesium rate, while cobalt(II), nickel(II), and strontium support the reaction at much lower rates (17,7, and 3%, respectively) (15). In A. calcoaceticus, both manganese(II) (14%) and cobalt(II) (12%) support a much lower reaction rate than magnesium.…”

Section: Discussionmentioning

confidence: 99%

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Purification and characterization of Acinetobacter calcoaceticus isocitrate lyase

1991

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Acinetobacter calcoacetius is capable of growing on acetate or compounds that are metabolized to acetate. During adaptation to growth on acetate, A. calcoaceticus B4 exhibits an increase in NADP+-isocitrate dehydrogenase and isocitrate lyase activities. In contrast, during adaptation to growth on acetate, Escherichia coli exhibits a decrease in NADP+-isocitrate dehydrogenase activity that is caused by reversible phosphorylation of specific serine residues on this enzyme. Also, in E. coli, isocitrate lyase is believed to be active only in the phosphorylated form. This phosphorylation of isocitrate lyase may regulate entry of isocitrate into the glyoxylate bypass. To understand the relationships between these two isocitrate-metabolizing enzymes and the metabolism of acetate in A. calcoaceticus B4 better, we have purified isocitrate lyase to homogeneity. Physical and kinetic characterization of the enzyme as well as the inhibitor specificity and divalent cation requirement have been examined.

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Section: Discussionsupporting

confidence: 59%

Section: Discussionmentioning

confidence: 83%

Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

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Purification and characterization of Acinetobacter calcoaceticus isocitrate lyase

1991

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“…A variety of metal ion combinations were studied for their ability to inhibit ICL activity. It is known for the isocitrate lyases of Corynebacterium glutamicum and Acinetobacter calcoaceticus that Mn 2+ can partially substitute for Mg 2+ (Hoyt et al, 1988;Hoyt et al, 1991).In the absence of divalent cations only negligible activity was measured for the purified MS. Mg 2+ at 5 mM was found to be the most effective cation. Mn 2+ was able to replace Mg 2+ , yielding 40% of the activity obtained with Mg 2+ , Co 2+ , Fe 2+ , Ca 2+ , Ba 2+ , Ni 2+ , Cd 2+ , Zn 2+ , Cu 2+ , and Hg 2+ were not able to support significant MS activity (Smith et al, 2003).…”

Section: Magnesium the Magic Molecule In Metabolic Recessionmentioning

confidence: 99%

Mycobacterium tuberculosis: Dormancy, Persistence and Survival in the Light of Protein Synthesis

Kumar¹,

Sanyal²

2012

Understanding Tuberculosis - Deciphering the Secret Life of the Bacilli

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Mycobacterium tuberculosis isocitrate lyase (MtbIcl): Role of divalent cations in modulation of functional and structural properties

Kumar¹,

Bhakuni²

2008

Proteins

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Isocitrate lyase (Icl), an enzyme that plays an important role in the regulation of isocitrate flux and anaplerotic replenishment of pool of substrate required for biosynthetic process in Mycobacterium tuberculosis is a potential drug target for the antituberculosis drugs. Divalent cations induce differential effect of activation and inhibition of MtbIcl functional activity. The study for the first time demonstrates that interaction of cations with MtbIcl results in differential modulation of the enzyme structure which is probably the underlying mechanism for differential modulation of functional activity of enzyme by divalent cations. The Mg(2+) and Mn(2+) ions act as activators of the enzyme and in their absence no enzymatic activity was observed. These cations do not induce any significant structural alteration in the enzyme as observed by far-UV CD and solvent denaturation studies using chaotropic salts. However, the thermal denaturation studies demonstrate that they do interact with the noncatalytic alpha/beta barrel core domain of the enzyme and destabilize it. The inhibitors Zn(2+) and Cd(2+) interact directly with the catalytic domain of the enzyme and unfold it as a result of which complete loss of the enzymatic activity is observed in their presence. The results obtained from the studies provide intriguing insight into the possible mechanism of divalent cation-induced changes in structure, function, and stability of MtbIcl.

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Escherichia coli isocitrate lyase: properties and comparisons

Cited by 19 publications

References 30 publications

Purification and characterization of Acinetobacter calcoaceticus isocitrate lyase

Purification and characterization of Acinetobacter calcoaceticus isocitrate lyase

Mycobacterium tuberculosis: Dormancy, Persistence and Survival in the Light of Protein Synthesis

Mycobacterium tuberculosis isocitrate lyase (MtbIcl): Role of divalent cations in modulation of functional and structural properties

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