Browsing GGNB - Göttinger Graduiertenzentrum für Neurowissenschaften, Biophysik und molekulare Biowissenschaften by Advisor "Tittmann, Kai Prof. Dr."
Now showing items 1-9 of 9
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New redox-switches in proteins
(2024-04-26)Regulation of cellular pathways in response to the redox state of a cell is an important regulatory process. A well-established paradigm of redox-sensing is disulfide formation between two cysteine residues and cysteine ... -
Mechanistic and structural characterization of human L-asparaginases
(2024-04-04)L-asparaginases are therapeutic proteins against acute lymphoblastic leukaemia (ALL), especially in children. As lymphoblastic cells depend on L-asparagine in the blood serum, its depletion by L-asparaginases leads to ... -
Reaction mechanism of hOMPD and CaAAD at atomic resolution
(2019-12-12)Decarboxylation reactions are fundamental processes in the chemistry of the animated world. Thus, the evolution of decarboxylases brought up a stunning array of diverse enzymes utilizing a variety of different mechanisms ... -
Phosphoketolase - A mechanistic update
(2018-08-22)The thiamine diphosphate (ThDP)-dependent enzyme phosphoketolase catalyzes the phosphorolytic cleavage of fructose-6-phosphate and/or xylulose 5-phosphate under the generation of the high-energy metabolite acetyl phosphate, ... -
Mechanistic Characterization of Transaldolase from <i>Thermoplasma Acidophilum</i> and Preliminary Analysis of the QncN/L-M Protein System from <i>Streptomyces Melanovinaceus</i>
(2018-02-13)The results introduced in the present work are mainly based on the pre-steady state and steady-state analysis supported by structural information from crystallographic studies. Different variants of TacTAL were generated ... -
Structural and biophysical characterization of human pyruvate dehydrogenase multi-enzyme complex
(2017-11-24)Pyruvate dehydrogenase multi-enzyme complex (PDHc) is an assembly of multiple copies of four different proteins. Together they carry out the oxidative decarboxylation of pyruvate and generate acetyl-CoA and NADH, which are ... -
Structure and Mechanism of the Flavoenzyme Lipoamide Dehydrogenase from Escherichia coli
(2016-08-29)The flavoenzyme lipoamide dehydrogenase (E3) is an ubiquitously distributed enzyme which is part of several multienzyme complexes involved in cellular carbon metabolism thus contributing to cellular homeostasis. It catalyzes ... -
Functional characterization of transketolase-like proteins and related model systems with respect to thiamin diphosphate mediated chemistry
(2014-11-12)Transketolases (TKTs, E.C 2.2.1.1) are ubiquitous distributed enzymes among all three domains of life. TKTs require thiamin diphosphate (ThDP) and bivalent cations as catalytic cofactors. They fulfill their catalytic ... -
Catalysis at the Interface- Elucidation of the Activation Process and Coupling of Catalysis and Compartmentalization of the Peripheral Membrane Protein Pyruvate Oxidase from Escherichia coli
(2014-02-06)The thiamine- and flavin-dependent peripheral membrane protein pyruvate oxidase from E. coli (EcPOX) catalyzes the oxidative decarboxylation of the central metabolite pyruvate to CO2 and acetate with a concomitant electron ...