Ulrich Menge

Helmholtz Centre for Infection Research

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Leopold Flohé

University of Padua

Hans‐Jürgen Hecht

Helmholtz Centre for Infection Research

Dirk Krumme

Helmholtz Centre for Infection Research

Helena Sztajer

Technische Universität Braunschweig

Rolf D. Schmid

University of Stuttgart

Josef Wissing

Helmholtz Centre for Infection Research

Heike Budde

Max Planck Institute for Biology

Everson Nogoceke

Roche (Switzerland)

Sergio A. Guerrero

Instituto de Agrobiotecnología del Litoral

Fragiskos N. Kolisis

National Technical University of Athens

Cooperative Institutions

Helmholtz Centre for Infection Research

Technische Universität Braunschweig

German Respiratory Society

Gesellschaft zur Förderung von Medizin-, Bio- und Umwelttechnologien

Centre National de la Recherche Scientifique

University of York

University of Münster

Novo Nordisk (Denmark)

University of Würzburg

Heinrich Heine University Düsseldorf

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Convenient Isolation and Kinetic Mechanism of Glutathionylspermidine Synthetase from Crithidia fasciculata

Journal of Biological Chemistry (1997)

Kerstin Koenig Ulrich Menge Michael Kieß Victor Wray Leopold Flohé

Trypanothione, the essential metabolite in the oxidant defense system of trypanosomatids, is synthesized by two distinct proteins, glutathionylspermidine synthetase and trypanothione synthetase. Glutathionylspermidine synthetase was purified to homogeneity from the trypanosomatid Crithidia fasciculataby aqueous two-phase systems and chromatography. The enzyme showed a specific activity of 38 μmol of glutathionylspermidine formed per min per mg of protein. Its molecular mass was 78 kDa in SDS-polyacrylamide gel electrophoresis, and it appeared predominantly monomeric in native polyacrylamide gel electrophoresis and gel filtration. The isoelectric point was at pH 4.6, and the pH optimum was near 7.6. Partial amino acid sequencing revealed homology with, but low similarity to, the glutathionylspermidine synthetase/amidase of Escherichia coli, and amidase activity was not detected in glutathionylspermidine synthetase of C. fasciculata. The kinetics of trypanosomatid glutathionylspermidine synthetase revealed a rapid equilibrium random mechanism with limiting K _m values for Mg²⁺-ATP, GSH, and spermidine of 0.25 ± 0.02, 2.51 ± 0.33, and 0.47 ± 0.09 mm, respectively, and a k _cat of 415 ± 78 min⁻¹. Partial reactions at restricted cosubstrate supply were not detected by ³¹P NMR, supporting the necessity of a quarternary complex formation for catalysis. ADP inhibited competitively with respect to ATP (K _i = 0.08 mm) and trypanothione exerted a feedback inhibition competitive with GSH (K _i = 0.48 mm).

Crithidia fasciculata

Isolation

Crithidia

10.1074/jbc.272.18.11908

Cite

Citations (48)

STRUCTURE OF TRYPAREDOXIN II

B. Hofmann H. Budde Karsten Bruns Sergio A. Guerrero Henryk M. Kalisz

10.2210/pdb1fg4/pdb

Cite

Citations (0)

Valdiation of Trypanosoma brucei trypanothione synthetase as drug target

Free Radical Biology and Medicine (2004)

Marcelo A. Comini Sergio A. Guerrero Simon Haile Ulrich Menge Heinrich Lünsdorf

10.1016/j.freeradbiomed.2004.02.008

Cite

Citations (104)

Towards novel biocatalysts via protein design: the case of lipases

FEMS Microbiology Reviews (1995)

Rolf D. Schmid Ulrich Menge Dietmar Schomburg Fritz Spener

During the past 3 years, the tertiary structures of several lipases have been solved by X-ray analysis. The structures revealed unique features such as hydrophobic ‘patches’ on the surface, presumably involved in lipid supersubstrate binding, and a lid structure which covers the active site in the absence of substrate. Only very recently the first X-ray structure of a bacterial lipase has been solved, and further structural features different from lipases of eukaryotic origin became apparent. Many lipase genes have been cloned and sequenced recently, and expression systems for the preparation of recombinant enzymes in good yields are available. As an example, the lipase from Rhizopus oryzae has been successfully expressed by us in Escherichia coli, and the resulting inclusion bodies were renatured in high yields. Consequently, the mechanism of action of lipases is now being studied via site-directed mutagenesis, and the rational design of lipases for the selective transformation of substrates is presently addressed in several laboratories.

Protein Engineering

Rhizopus oryzae

Rational design

Protein design

10.1111/j.1574-6976.1995.tb00172.x

Cite

Citations (5)

Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis

Archives of Biochemistry and Biophysics (2004)

Timo Jaeger Heike Budde Leopold Flohé Ulrich Menge Mahavir Singh

Peroxiredoxin

Ferredoxin-thioredoxin reductase

10.1016/j.abb.2003.11.021

Cite

Citations (158)

Influence of temperature and oil-to-surfactant ratio on micellar growth in aqueous solutions of C12E5 with decane

Colloids and Surfaces A Physicochemical and Engineering Aspects (2000)

Ulrich Menge Peter R. Lang Gerhard H. Findenegg

Microemulsion

Decane

Mass fraction

Molar mass

Micellar solutions

Mole fraction

10.1016/s0927-7757(99)00433-1

Cite

Citations (24)

Optimised fermentation strategy for 13C/15N recombinant protein labelling in Escherichia coli for NMR-structure analysis

Journal of Biotechnology (2004)

Anton Roß Waltraud Kessler Dirk Krumme Ulrich Menge Josef Wissing

Crithidia fasciculata

Ammonium sulfate

Metabolic flux analysis

10.1016/j.jbiotec.2003.10.014

Cite

Citations (13)

Die dialektische Struktur der Kurzgeschichten Dona Emilia Pardo Bazans

Hispanic Review (1970)

Juan Cano Ballesta Ulrich Menge

10.2307/471901

Cite

Citations (0)

Purification and some properties of formamidase from rat and pig liver.

PubMed (1975)

K Krisch R. Arndt Wolfgang Junge Ulrich Menge Konrad Michelssen

Formamidase was purified 4700-fold from rat liver cytoplasma. Its main molecular and catalytic properties are reported. In pig liver three active forms were observed.

Source

Cite

Citations (6)

Synthesis of structured triglycerides from peanut oil with immobilized lipase

Journal of the American Oil Chemists Society (1997)

Mohamed M. Soumanou Uwe T. Bornscheuer Ulrich Menge Rolf D. Schmid

Abstract Structured triglycerides (ST) that contain medium‐ and long‐chain fatty acids were synthesized by lipase‐catalyzed interesterification between tricaprylin and peanut oil. To select appropriate enzymes, we investigated nine commercial lipase preparations for their ability to hydrolyze pure triglycerides as well as natural oils. Three microbial lipases from Rhizomucor miehei (RML), Candida sp. (CSL), and Chromobacterium viscosum (CVL) gave good results, and immobilized preparations were used in the interesterification. RML gave the highest yields of ST (73%, 40°C), although its hydrolytic activity toward triolein was low. As the temperature was raised to 50°C, the yield of ST increased to 79%. After 120 h reaction time, remaining activities were high for CSL (71%), moderate for CVL (48%), and low for RML (20%).

Interesterified fat

Triolein

Rhizomucor miehei

Peanut oil

10.1007/s11746-997-0101-5

Cite

Citations (60)