Characterization of acetohydroxy acid synthase activity in the archaeon Haloferax volcanii

Maria Vyazmensky; Ze'ev Barak; David M. Chipman; Jerry Eichler

doi:10.1016/S0305-0491(99)00170-4

Characterization of acetohydroxy acid synthase activity in the archaeon Haloferax volcanii

Maria Vyazmensky, Ze'ev Barak, David M. Chipman, Jerry Eichler

Department of Life Sciences

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

6 Scopus citations

Abstract

Whereas the biochemistry of acetohydroxy acid synthase has been extensively studied in bacteria and eukaryotes, relatively little is known about the enzyme in archaea, the third kingdom of life. The present study biochemically characterizes acetohydroxy acid synthase activity in the halophilic archaea Haloferax volcanii. In addressing ion requirements, enzyme inhibition and antibody labeling, the results reveal that, except for its elevated salt requirements, the haloarchaeal enzyme is remarkably similar to its bacterial counterpart. Copyright (C) 2000 Elsevier Science Inc.

Original language	English
Pages (from-to)	205-210
Number of pages	6
Journal	Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume	125
Issue number	2
DOIs	https://doi.org/10.1016/S0305-0491(99)00170-4
State	Published - 1 Jan 2000

Keywords

Acetohydroxy acid synthase
Amino acid biosynthesis
Archaea
Branched-chain amino acids
Euryarchaeota
Haloferax volcanii
Halophile

ASJC Scopus subject areas

Biochemistry
Physiology
Molecular Biology

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10.1016/S0305-0491(99)00170-4

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title = "Characterization of acetohydroxy acid synthase activity in the archaeon Haloferax volcanii",

abstract = "Whereas the biochemistry of acetohydroxy acid synthase has been extensively studied in bacteria and eukaryotes, relatively little is known about the enzyme in archaea, the third kingdom of life. The present study biochemically characterizes acetohydroxy acid synthase activity in the halophilic archaea Haloferax volcanii. In addressing ion requirements, enzyme inhibition and antibody labeling, the results reveal that, except for its elevated salt requirements, the haloarchaeal enzyme is remarkably similar to its bacterial counterpart. Copyright (C) 2000 Elsevier Science Inc.",

keywords = "Acetohydroxy acid synthase, Amino acid biosynthesis, Archaea, Branched-chain amino acids, Euryarchaeota, Haloferax volcanii, Halophile",

author = "Maria Vyazmensky and Ze'ev Barak and Chipman, {David M.} and Jerry Eichler",

note = "Funding Information: This work was supported by grants from the Israel Science Foundation (#243/98 to Z.B. and D.M.C.) and the Israel Ministry of Absorption (M.V. and J.E.).",

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T1 - Characterization of acetohydroxy acid synthase activity in the archaeon Haloferax volcanii

AU - Vyazmensky, Maria

AU - Barak, Ze'ev

AU - Chipman, David M.

AU - Eichler, Jerry

N1 - Funding Information: This work was supported by grants from the Israel Science Foundation (#243/98 to Z.B. and D.M.C.) and the Israel Ministry of Absorption (M.V. and J.E.).

PY - 2000/1/1

Y1 - 2000/1/1

N2 - Whereas the biochemistry of acetohydroxy acid synthase has been extensively studied in bacteria and eukaryotes, relatively little is known about the enzyme in archaea, the third kingdom of life. The present study biochemically characterizes acetohydroxy acid synthase activity in the halophilic archaea Haloferax volcanii. In addressing ion requirements, enzyme inhibition and antibody labeling, the results reveal that, except for its elevated salt requirements, the haloarchaeal enzyme is remarkably similar to its bacterial counterpart. Copyright (C) 2000 Elsevier Science Inc.

AB - Whereas the biochemistry of acetohydroxy acid synthase has been extensively studied in bacteria and eukaryotes, relatively little is known about the enzyme in archaea, the third kingdom of life. The present study biochemically characterizes acetohydroxy acid synthase activity in the halophilic archaea Haloferax volcanii. In addressing ion requirements, enzyme inhibition and antibody labeling, the results reveal that, except for its elevated salt requirements, the haloarchaeal enzyme is remarkably similar to its bacterial counterpart. Copyright (C) 2000 Elsevier Science Inc.

KW - Acetohydroxy acid synthase

KW - Amino acid biosynthesis

KW - Archaea

KW - Branched-chain amino acids

KW - Euryarchaeota

KW - Haloferax volcanii

KW - Halophile

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U2 - 10.1016/S0305-0491(99)00170-4

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M3 - Article

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JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

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Characterization of acetohydroxy acid synthase activity in the archaeon Haloferax volcanii

Abstract

Keywords

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