Search Results - "Spinka, Michael"
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Arabidopsis thaliana PECP1 — Enzymatic characterization and structural organization of the first plant phosphoethanolamine/phosphocholine phosphatase
Published in Biochimica et biophysica acta (01-02-2012)“…Maintenance of cellular phosphate homeostasis is crucial for primary and energy metabolism. In plants, low exogenous phosphate availability activates adaptive…”
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Journal Article -
2
Significance of Individual Residues at the Regulatory Site of Yeast Pyruvate Decarboxylase for Allosteric Substrate Activation
Published in Biochemistry (Easton) (07-03-2017)“…The catalytic activity of the allosteric enzyme pyruvate decarboxylase from yeast is strictly controlled by its own substrate pyruvate via covalent binding at…”
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Journal Article -
3
Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation
Published in The Journal of biological chemistry (01-05-2009)“…The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven…”
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Journal Article -
4
Activation of Thiamin Diphosphate and FAD in the Phosphatedependent Pyruvate Oxidase fromLactobacillus plantarum
Published in The Journal of biological chemistry (22-05-1998)“…The phosphate- and oxygen-dependent pyruvate oxidase from Lactobacillus plantarum is a homotetrameric enzyme that binds 1 FAD and 1 thiamine diphosphate per…”
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Journal Article -
5
Phosphorylation of Serine 264 Impedes Active Site Accessibility in the E1 Component of the Human Pyruvate Dehydrogenase Multienzyme Complex
Published in Biochemistry (Easton) (29-05-2007)“…At the junction of glycolysis and the Krebs cycle in cellular metabolism, the pyruvate dehydrogenase multienzyme complex (PDHc) catalyzes the oxidative…”
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Journal Article -
6
Allosteric activation of pyruvate decarboxylases. A never-ending story?
Published in Journal of molecular catalysis. B, Enzymatic (01-11-2009)“…The allosteric substrate activation of pyruvate decarboxylases was studied for more than 30 years using varying techniques and ending up in different…”
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Journal Article Conference Proceeding -
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Catalytically active filaments – pyruvate decarboxylase from Neurospora crassa. pH‐controlled oligomer structure and catalytic function
Published in The FEBS journal (01-01-2012)“…Pyruvate decarboxylase is a key enzyme in organisms whose energy metabolism is based on alcoholic fermentation. The enzyme catalyses the nonoxidative…”
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Journal Article -
8
Catalytically active filaments - pyruvate decarboxylase from Neurosporacrassa. pH-controlled oligomer structure and catalytic function
Published in The FEBS journal (01-01-2012)“…Pyruvate decarboxylase is a key enzyme in organisms whose energy metabolism is based on alcoholic fermentation. The enzyme catalyses the nonoxidative…”
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Journal Article -
9
Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme ActivationS
Published in The Journal of biological chemistry (01-05-2009)“…The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven…”
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Journal Article -
10
Amino Acids Allosterically Regulate the Thiamine Diphosphate-dependent α-Keto Acid Decarboxylase from Mycobacterium tuberculosis
Published in The Journal of biological chemistry (29-02-2008)“…The gene rv0853c from Mycobacterium tuberculosis strain H37Rv codes for a thiamine diphosphate-dependent α-keto acid decarboxylase (MtKDC), an enzyme involved…”
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Journal Article -
11
Amino Acids Allosterically Regulate the Thiamine Diphosphate-dependent α-Keto Acid Decarboxylase from Mycobacterium tuberculosis
Published in The Journal of biological chemistry (29-02-2008)“…The gene rv0853c from Mycobacterium tuberculosis strain H37Rv codes for a thiamine diphosphate-dependent α-keto acid decarboxylase ( Mt KDC), an enzyme…”
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Journal Article -
12
The influence of protein concentration on oligomer structure and catalytic function of two pyruvate decarboxylases
Published in The Protein Journal (01-12-2007)“…As a general rule protein concentration typical for structural studies differs considerably from that chosen for kinetic investigations. Consequently,…”
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Journal Article -
13
Consequences of a Modified Putative Substrate-Activation Site on Catalysis by Yeast Pyruvate Decarboxylase
Published in Biochemistry (Easton) (13-02-2001)“…Earlier, it had been proposed in the laboratories at Halle that a cysteine residue is responsible for the hysteretic substrate activation behavior of yeast…”
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Journal Article -
14
Activation of Thiamin Diphosphate and FAD in the Phosphate-dependent Pyruvate Oxidase from Lactobacillus plantarum
Published in The Journal of biological chemistry (22-05-1998)“…The phosphate- and oxygen-dependent pyruvate oxidase from Lactobacillus plantarum is a homotetrameric enzyme that binds 1 FAD and 1 thiamine diphosphate per…”
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Journal Article -
15
Pyruvate decarboxylase from Kluyveromyces lactis. An enzyme with an extraordinary substrate activation behaviour
Published in European journal of biochemistry (01-07-2002)“…Pyruvate decarboxylase (EC 4.1.1.1) was isolated and purified from the yeast Kluyveromyces lactis. The properties of this enzyme relating to the native…”
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Journal Article -
16
Molecular Mechanism of Regulation of the Pyruvate Dehydrogenase Complex from E. coli
Published in Biochemistry (Easton) (16-12-1997)“…The pyruvate dehydrogenase multienzyme complex from E. coli shows a sigmoidal dependency of the reaction rate on the substrate concentration when product…”
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Journal Article -
17
Pyruvate decarboxylase from Kluyveromyces lactis
Published in European journal of biochemistry (01-07-2002)“…Pyruvate decarboxylase (EC 4.1.1.1) was isolated and purified from the yeast Kluyveromyces lactis. The properties of this enzyme relating to the native…”
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Journal Article -
18
Activation of thiamin diphosphate in enzymes
Published in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology (29-06-1998)“…Activation of the coenzyme ThDP was studied by measuring the kinetics of deprotonation at the C2 carbon of thiamin diphosphate in the enzymes pyruvate…”
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