D. Kessler

Heinrich Heine University Düsseldorf

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Tim Clausen

Research Institute of Molecular Pathology

J.T. Kaiser

Gesundes Kinzigtal (Germany)

G. Fischer

RWTH Aachen University

Georg E. Schulz

University of Freiburg

Jürgen Ramharter

Boehringer Ingelheim (Austria)

Guido J. Reiß

Heinrich Heine University Düsseldorf

Clemens Steegborn

University of Bayreuth

János Rétey

Karlsruhe Institute of Technology

R. Huber

Max Planck Institute of Biochemistry

Meike Burow

University of Copenhagen

Cooperative Institutions

Max Planck Society

University of Parma

University of Vienna

Ghent University

University of California, Davis

Martin Luther University Halle-Wittenberg

University of Verona

University of Freiburg

National Institutes of Health

Heidelberg University

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Enzymatic Activity of the Arabidopsis Sulfurtransferase Resides in the C-Terminal Domain But Is Boosted by the N-Terminal Domain and the Linker Peptide in the Full- Length Enzyme

Biological Chemistry (2002)

Meike Burow D. Kessler Jutta Papenbrock

Sulfurtransferases/rhodaneses are a group of enzymes widely distributed in plants, animals, and bacteria that catalyze the transfer of sulfur from a donor molecule to a thiophilic acceptor substrate. Sulfurtransferases (STs) consist of two globular domains of nearly identical size and conformation connected by a short linker sequence. In plant STs this linker sequence is exceptionally longer than in sequences from other species. The Arabidopsis ST1 protein (AJ131404) contains five cysteine residues: one residue is universally conserved in all STs and considered to be catalytically essential; a second one, closely located in the primary sequence, is conserved only in sequences from eukaryotic species. Of the remaining three cysteine residues two are conserved in the so far known plant STs and one is unique to the Arabidopsis ST1. The aim of our study was to investigate the role of the twodomain structure, of the unique plant linker sequence and of each cysteine residue. The N and Cterminal domains of the Arabidopsis ST1, the fulllength protein with a shortened linker sequence and several pointmutated proteins were overexpressed in E. coli, purified and used for enzyme activity measurements. The Cterminal domain itself displayed ST activity which could be increased by adding the separately prepared Nterminal domain. The activity of an ST1 derivative with a shortened linker sequence was reduced by more than 60% of the wildtype activity, probably because of a drastically reduced protein stability. The replacement of each cysteine residue resulted in mutant forms which differed significantly in their stability, in the specific ST activities, and in their kinetic parameters which were determined for 3-mercaptopyruvate as well as thiosulfate as sulfur substrates: mutation of the putative active site cysteine (C332) essentially abolished activity; for C339 a crucial role at least for the turnover of thiosulfate could be identified.

Linker

Residue (chemistry)

10.1515/bc.2002.155

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Citations (9)

CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES

Tim Clausen J.T. Kaiser Clemens Steegborn R. Huber D. Kessler

Lyase

Crystal (programming language)

10.2210/pdb1elq/pdb

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The High Resolution Structure of Urocanate Hydratase from Pseudomonas putida in complex with urocanate

D. Kessler János Rétey Georg E. Schulz

Pseudomonas putida

Pseudomonadales

10.2210/pdb1uwk/pdb

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Crystal structure of bis((dimethylphosphoryl)methanaminium) hexachloridoiridate( IV), C6H22Cl6IrN2O2P2

Zeitschrift für Kristallographie - New Crystal Structures (2014)

D. Kessler Guido J. Reiß

Abstract C 6 H 22 Cl 6 IrN 2 O 2 P 2 , monoclinic, P2 1 /c (no. 14), a = 7.1388(3) Å, b = 13.7576(5) Å, c = 10.0474(4) Å, β = 104.972(4)°, V = 953.3 Å 3 , Z = 2, R gt (F) = 0.0150, wR ref (F 2 ) = 0.0384, T = 295 K.

Monoclinic crystal system

Crystal (programming language)

10.1515/ncrs-2014-0054

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Citations (1)

1.76A Structure of Urocanate Hydratase from Pseudomonas putida

D. Kessler János Rétey Georg E. Schulz

Pseudomonas putida

10.2210/pdb1uwl/pdb

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COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.

Tim Clausen J.T. Kaiser Clemens Steegborn R.E. Huber D. Kessler

Lyase

10.2210/pdb1elu/pdb

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SOS1 in Complex with Inhibitor BI-68BS

D. Kessler G. Fischer Jürgen Ramharter

10.2210/pdb6sfr/pdb

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SOS1 in Complex with Inhibitor BI-3406

D. Kessler G. Fischer Jürgen Ramharter

10.2210/pdb6scm/pdb

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Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymic AdhE protein of Escherichia coli.

Journal of Biological Chemistry (1992)

D. Kessler W. Herth J Knappe

The AdhE protein of Escherichia coli is a homopolymer of 96-kDa subunits harboring three Fe(2+)-dependent catalytic functions: acetaldehyde-CoA dehydrogenase, alcohol dehydrogenase, and pyruvate formatelyase (PFL) deactivase. By negative staining electron microscopy, we determined a helical assembly of 20-60 subunits into rods of 45-120 nm in length. The subunit packing is widened along the helix axis when Fe2+ and NAD are present. Chymotrypsin dissects the AdhE polypeptide between Phe762 and Ser763, thereby retaining the alcohol dehydrogenase activity on the NH2-terminal core, but destroying all other activities. PFL deactivation, i.e. quenching of the glycyl radical in PFL by the AdhE protein, was examined with respect to cofactor involvements (Fe2+, NAD, and CoA). This process is coupled to NAD reduction and requires the intact CoA sulfhydryl group. Pyruvate and NADH are inhibitors that affect the steady-state level of the radical form of PFL in a reconstituted interconversion cycle. Studies of cell cultures found that PFL deactivation in situ is initiated at redox potentials of greater than or equal to +100 mV. Our results provide insights into the structure/function organization of the AdhE multienzyme and give a rationale for how its PFL radical quenching activity may be suppressed in situ to enable effective glucose fermentation.

10.1016/s0021-9258(19)37154-6

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Citations (125)

Structure of A Catalytically Inactive Mutant (K223A) of C-DES with a Substrate (Cystine) Linked to the Co-Factor

J.T. Kaiser Stefano Bruno Tim Clausen R. Huber Francesca Schiaretti

10.2210/pdb1n31/pdb

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