Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

Helge Uhrigshardt; Michael Walden; Harald John; Arnd Petersen; Stefan Anemüller

doi:10.1016/S0014-5793(02)02317-7

Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

Helge Uhrigshardt, Michael Walden, Harald John, Arnd Petersen, Stefan Anemüller^*

^*Corresponding author for this work

Institute of Biochemistry

22 Citations (Scopus)

Abstract

Both key enzymes for the glyoxylate cycle, isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2), were purified and characterized from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Whereas the former enzyme was copurified with the aconitase, the latter enzyme could be enriched to apparent homogeneity. Amino acid sequencing of three internal peptides of the isocitrate lyase revealed the presence of highly conserved residues. With respect to cofactor requirement and quarternary structure the crenarchaeal malate synthase might represent a novel type of this enzyme family. High activities of both glyoxylate cycle enzymes could already be detected in extracts of glucose grown cells and both increased about two-fold in extracts of acetate grown cells.

Original language	English
Journal	FEBS Letters
Volume	513
Issue number	2-3
Pages (from-to)	223-229
Number of pages	7
ISSN	0014-5793
DOIs	https://doi.org/10.1016/S0014-5793(02)02317-7
Publication status	Published - 27.02.2002

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Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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title = "Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius",

abstract = "Both key enzymes for the glyoxylate cycle, isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2), were purified and characterized from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Whereas the former enzyme was copurified with the aconitase, the latter enzyme could be enriched to apparent homogeneity. Amino acid sequencing of three internal peptides of the isocitrate lyase revealed the presence of highly conserved residues. With respect to cofactor requirement and quarternary structure the crenarchaeal malate synthase might represent a novel type of this enzyme family. High activities of both glyoxylate cycle enzymes could already be detected in extracts of glucose grown cells and both increased about two-fold in extracts of acetate grown cells.",

author = "Helge Uhrigshardt and Michael Walden and Harald John and Arnd Petersen and Stefan Anem{\"u}ller",

note = "Funding Information: This work was supported by a Grant form the Deutsche Forschungsgemeinschaft (An 194/2-1/2). The authors would like to thank Prof. G. Sch{\"a}fer and Dr. R. Moll for critical discussion of the manuscript, Mrs. Susanne Zoske (Medical University L{\"u}beck), Mrs. Jutta Barras-Aknoukh and Mrs. Stefanie Schulz (both IPF PharmaCeuticals) for excellent technical assistance. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",

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doi = "10.1016/S0014-5793(02)02317-7",

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T1 - Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

AU - Uhrigshardt, Helge

AU - Walden, Michael

AU - John, Harald

AU - Petersen, Arnd

AU - Anemüller, Stefan

N1 - Funding Information: This work was supported by a Grant form the Deutsche Forschungsgemeinschaft (An 194/2-1/2). The authors would like to thank Prof. G. Schäfer and Dr. R. Moll for critical discussion of the manuscript, Mrs. Susanne Zoske (Medical University Lübeck), Mrs. Jutta Barras-Aknoukh and Mrs. Stefanie Schulz (both IPF PharmaCeuticals) for excellent technical assistance. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

PY - 2002/2/27

Y1 - 2002/2/27

N2 - Both key enzymes for the glyoxylate cycle, isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2), were purified and characterized from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Whereas the former enzyme was copurified with the aconitase, the latter enzyme could be enriched to apparent homogeneity. Amino acid sequencing of three internal peptides of the isocitrate lyase revealed the presence of highly conserved residues. With respect to cofactor requirement and quarternary structure the crenarchaeal malate synthase might represent a novel type of this enzyme family. High activities of both glyoxylate cycle enzymes could already be detected in extracts of glucose grown cells and both increased about two-fold in extracts of acetate grown cells.

AB - Both key enzymes for the glyoxylate cycle, isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2), were purified and characterized from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Whereas the former enzyme was copurified with the aconitase, the latter enzyme could be enriched to apparent homogeneity. Amino acid sequencing of three internal peptides of the isocitrate lyase revealed the presence of highly conserved residues. With respect to cofactor requirement and quarternary structure the crenarchaeal malate synthase might represent a novel type of this enzyme family. High activities of both glyoxylate cycle enzymes could already be detected in extracts of glucose grown cells and both increased about two-fold in extracts of acetate grown cells.

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Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

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