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Dive into the research topics where Halina Szadkowski is active.

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Featured researches published by Halina Szadkowski.


Journal of Molecular Biology | 1980

Limited proteolysis of N-(5′-phosphoribosyl)anthranilate isomerase: Indoleglycerol phosphate synthase from Escherichia coli yields two different enzymically active, functional domains☆

Kasper Kirschner; Halina Szadkowski; Agnes Henschen; Friedrich Lottspeich

Abstract The native enzyme must be denatured either by sodium dodecyl sulfate or by urea before limited proteolysis can occur. Under these conditions only one or two peptide bonds are hydrolyzed by each of the following proteases: Staphylococcal V8 protease, trypsin and elastase. The amino-terminal amino acid sequences were determined to identify the cleavage sites. The new sequences comprise approximately 20% of the entire polypeptide chain, and show good agreement with the nucleotide sequence of the trpC gene. Both V8 protease † and elastase yield large carboxy-terminal fragments, about two thirds of the size of the parent enzyme, and corresponding small amino-terminal fragments. Trypsin cleaves a single peptide bond in the last one third of the polypeptide chain. After separation of the fragments, removal of dodecyl sulfate and renaturation, only the large fragments fold to stable structures. The small fragments precipitate. The large amino-terminal fragment catalyzes only the synthesis of indoleglycerol phosphate and precipitates when solutions are frozen and thawed. The large carboxy-terminal fragment catalyzes only the isomerization of N-(5′-phosphoribosyl)anthranilate and is stable towards freezing and thawing. These studies prove that the intact bifunctional enzyme consists of two autonomously folding, functional domains. They also support the notion that the bifunctional enzyme may have arisen by the fusion of separate ancestral genes, and that stabilization of the intrinsically labile indoleglycerol phosphate synthase domain by interdomain interactions is functionally advantageous.


FEBS Journal | 1990

Protein-decorated micelle structure of sodium-dodecyl-sulfate--protein complexes as determined by neutron scattering.

Konrad Ibel; Roland P. May; Kasper Kirschner; Halina Szadkowski; Erik Mascher; Per Lundahl


Biochemistry | 2000

Improving the catalytic activity of a thermophilic enzyme at low temperatures.

Astrid Merz; Muh-Ching Yee; Halina Szadkowski; Günter Pappenberger; Andreas Crameri; Willem P. C. Stemmer; Charles Yanofsky; Kasper Kirschner


Protein Science | 1996

PHOSPHORIBOSYL ANTHRANILATE ISOMERASE FROM THERMOTOGA MARITIMA IS AN EXTREMELY STABLE AND ACTIVE HOMODIMER

Reinhard Sterner; G. R. Kleemann; Halina Szadkowski; Ariel Lustig; Michael Hennig; Kasper Kirschner


Biochemistry | 1992

A fully active variant of dihydrofolate reductase with a circularly permuted sequence

Anne Buchwalder; Halina Szadkowski; Kasper Kirschner


Methods in Enzymology | 1987

[48] Phosphoribosylanthranilate isomerase—indoleglycerol-phosphate synthase from Escherichia coli

Kasper Kirschner; Halina Szadkowski; Theodore S. Jardetzky; Vreni Hager


Protein Engineering | 1990

An 8-fold βα barrel protein with redundant folding possibilities

Karolin Luger; Halina Szadkowski; Kasper Kirschner


FEBS Journal | 2002

Stabilization of a (βα)8-barrel protein by an engineered disulfide bridge

Andreas Ivens; Olga Mayans; Halina Szadkowski; Catharina Jürgens; Matthias Wilmanns; Kasper Kirschner


Protein Science | 1998

Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli

Beatrice Darimont; Catherine Stehlin; Halina Szadkowski; Kasper Kirschner


FEBS Journal | 2001

Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus

Andreas Ivens; Olga Mayans; Halina Szadkowski; Matthias Wilmanns; Kasper Kirschner

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Matthias Wilmanns

European Bioinformatics Institute

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Olga Mayans

University of Liverpool

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Günter Pappenberger

Institute of Cancer Research

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