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^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biochemie

25 Zitate (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.

Originalsprache	Englisch
Zeitschrift	FEBS Letters
Jahrgang	513
Ausgabenummer	2-3
Seiten (von - bis)	223-229
Seitenumfang	7
ISSN	0014-5793
DOIs	https://doi.org/10.1016/S0014-5793(02)02317-7
Publikationsstatus	Veröffentlicht - 27.02.2002

Fördermittel

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.

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Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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10.1016/S0014-5793(02)02317-7

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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",

language = "English",

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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.

UR - https://www.scopus.com/pages/publications/0037181133

U2 - 10.1016/S0014-5793(02)02317-7

DO - 10.1016/S0014-5793(02)02317-7

M3 - Journal articles

C2 - 11904155

AN - SCOPUS:0037181133

SN - 0014-5793

VL - 513

SP - 223

EP - 229

JO - FEBS Letters

JF - FEBS Letters

IS - 2-3

ER -

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

Abstract

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