Isocitrate lyase activity in halophilic archaea

Aharon Oren; Peter Gurevich

doi:10.1016/0378-1097(95)00189-C

Isocitrate lyase activity in halophilic archaea

Aharon Oren^*, Peter Gurevich

^*Corresponding author for this work

Department of Plant and Environmental Sciences (Natural Sciences)

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Eight species of halophilic Archaea were tested for the presence of isocitrate lyase activity. High activities (up to 100 nmol min^-1 mg protein^-1) were detected in Haloferax mediterranei and Haloferax volcanii when grown in medium containing acetate as the principal carbon source. Little activity was found in representatives of the genera Halobacterium and Haloarcula. Isocitrate lyase from Haloferax mediterranei required high potassium chloride concentrations, optimal activity being found at 1.5-3 M potassium chloride and pH 7.0. Replacement of potassium chloride by sodium chloride resulted in much lower activities. Sulfhydryl compounds (cysteine, glutathione) were not stimulatory. In other properties (stimulation by magnesium ions, sensitivity to different inhibitors) the enzyme resembled isocitrate lyases from representatives of the Bacteria and Eucarya.

Original language	English
Pages (from-to)	91-95
Number of pages	5
Journal	FEMS Microbiology Letters
Volume	130
Issue number	1
DOIs	https://doi.org/10.1016/0378-1097(95)00189-C
State	Published - 15 Jul 1995

Bibliographical note

Funding Information:
This work was supported by a grant from the Israel Science Foundation administeredb y the Israel Academy of Sciences and Humanities.

Keywords

Acetate metabolism
Archaea
Halophilic
Isocitrate lyase

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10.1016/0378-1097(95)00189-C

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title = "Isocitrate lyase activity in halophilic archaea",

abstract = "Eight species of halophilic Archaea were tested for the presence of isocitrate lyase activity. High activities (up to 100 nmol min-1 mg protein-1) were detected in Haloferax mediterranei and Haloferax volcanii when grown in medium containing acetate as the principal carbon source. Little activity was found in representatives of the genera Halobacterium and Haloarcula. Isocitrate lyase from Haloferax mediterranei required high potassium chloride concentrations, optimal activity being found at 1.5-3 M potassium chloride and pH 7.0. Replacement of potassium chloride by sodium chloride resulted in much lower activities. Sulfhydryl compounds (cysteine, glutathione) were not stimulatory. In other properties (stimulation by magnesium ions, sensitivity to different inhibitors) the enzyme resembled isocitrate lyases from representatives of the Bacteria and Eucarya.",

keywords = "Acetate metabolism, Archaea, Halophilic, Isocitrate lyase",

author = "Aharon Oren and Peter Gurevich",

note = "Funding Information: This work was supported by a grant from the Israel Science Foundation administeredb y the Israel Academy of Sciences and Humanities.",

year = "1995",

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doi = "10.1016/0378-1097(95)00189-C",

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AU - Oren, Aharon

AU - Gurevich, Peter

N1 - Funding Information: This work was supported by a grant from the Israel Science Foundation administeredb y the Israel Academy of Sciences and Humanities.

PY - 1995/7/15

Y1 - 1995/7/15

N2 - Eight species of halophilic Archaea were tested for the presence of isocitrate lyase activity. High activities (up to 100 nmol min-1 mg protein-1) were detected in Haloferax mediterranei and Haloferax volcanii when grown in medium containing acetate as the principal carbon source. Little activity was found in representatives of the genera Halobacterium and Haloarcula. Isocitrate lyase from Haloferax mediterranei required high potassium chloride concentrations, optimal activity being found at 1.5-3 M potassium chloride and pH 7.0. Replacement of potassium chloride by sodium chloride resulted in much lower activities. Sulfhydryl compounds (cysteine, glutathione) were not stimulatory. In other properties (stimulation by magnesium ions, sensitivity to different inhibitors) the enzyme resembled isocitrate lyases from representatives of the Bacteria and Eucarya.

AB - Eight species of halophilic Archaea were tested for the presence of isocitrate lyase activity. High activities (up to 100 nmol min-1 mg protein-1) were detected in Haloferax mediterranei and Haloferax volcanii when grown in medium containing acetate as the principal carbon source. Little activity was found in representatives of the genera Halobacterium and Haloarcula. Isocitrate lyase from Haloferax mediterranei required high potassium chloride concentrations, optimal activity being found at 1.5-3 M potassium chloride and pH 7.0. Replacement of potassium chloride by sodium chloride resulted in much lower activities. Sulfhydryl compounds (cysteine, glutathione) were not stimulatory. In other properties (stimulation by magnesium ions, sensitivity to different inhibitors) the enzyme resembled isocitrate lyases from representatives of the Bacteria and Eucarya.

KW - Acetate metabolism

KW - Archaea

KW - Halophilic

KW - Isocitrate lyase

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ER -

Isocitrate lyase activity in halophilic archaea

Abstract

Bibliographical note

Keywords

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