A5004696341- Steroid Chemistry and Biochemistry
- Pharmacogenetics and Drug Metabolism
- Trypanosoma species research and implications
- Hormonal Regulation and Hypertension
- Microbial Metabolic Engineering and Bioproduction
- Calcium signaling and nucleotide metabolism
- Analytical Chemistry and Chromatography
- Personality Traits and Psychology
- Enzyme Catalysis and Immobilization
- Microbial Natural Products and Biosynthesis
- Process Optimization and Integration
- Paleontology and Evolutionary Biology
- Cellular transport and secretion
- Evolutionary Psychology and Human Behavior
- Research on Leishmaniasis Studies
- Insect Utilization and Effects
- Consumer Behavior in Brand Consumption and Identification
- Enzyme Structure and Function
- Lysosomal Storage Disorders Research
- Biochemical and Molecular Research
- Geological Formations and Processes Exploration
- Paleontology and Stratigraphy of Fossils
Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences
2019-2023
Max Perutz Labs
2020-2021
Medical University of Vienna
2020-2021
Vienna Biocenter
2021
Silesian University of Technology
2021
Uniwersytet SWPS
2015
Jagiellonian University
2003
Δ1-Dehydrogenation of 3-ketosteroids catalyzed by flavin adenine dinucleotide (FAD)-dependent 3-ketosteroid dehydrogenases (Δ1-KSTD) is a crucial step in steroid degradation and synthesis several drugs. The catalytic mechanism assumes the formation double bond two steps, proton abstraction tyrosyl ion, rate-limiting hydride transfer to FAD. This hypothesis was never verified quantum-mechanical studies despite contradictory results from kinetic isotope effect (KIE) reported 1960 Jerussi...
3-Ketosteroid Δ
Abstract Background 3-Ketosteroid Δ 1 -dehydrogenases (KSTDs) are the enzymes involved in microbial cholesterol degradation and modification of steroids. They catalyze dehydrogenation between C1 C2 atoms ring A polycyclic structure 3-ketosteroids. KSTDs substrate spectrum is broad, even though most them prefer steroids with small substituents at C17 atom. The investigation KSTD’s specificity hindered by poor solubility hydrophobic aqueous solutions. In this paper, we used...
This research aimed at obtaining new derivatives of pregn-1,4-diene-3,20-dione (Δ
Cholest-4-en-3-one Δ1-dehydrogenase (AcmB) from Sterolibacterium denitrificans was successfully immobilized on 3-aminopropyltrimethoysilane functionalized mesoporous cellular foam (MCF) and Santa Barbara Amorphous (SBA-15) silica supports using adsorption or covalently with glutaraldehyde divinyl sulfone linkers. The best catalyst, AcmB MCF linked glutaraldehyde, retained the specific activity of homogenous enzyme while exhibiting a substantial increase operational stability. used...
Cholest-4-en-3-one Δ1-dehydrogenase (AcmB) from Sterolibacterium denitrificans is successfully immobilized on 3-aminopropyltrimethoysilane functionalized MCF and SBA-15 silica supports using adsorption or covalently with glutaraldehyde divinyl sulfone linkers. The best catalyst, AcmB linked glutaraldehyde, retains the specific activity of homogenous enzyme while exhibiting a substantial increase operational stability. was used continuously in fed-batch reactor for 27 days,...
3-Ketosteroid Δ1-dehydrogenases (KstD) are important microbial flavin enzymes that initiate the metabolism of steroid ring A and useful find application in synthesis drugs. We present a structure KstD from Sterolibacterium denitrificans (AcmB), which contains previously uncharacterized membrane-associated domain extended proton-relay system. The experimental theoretical studies show 1,2-dehydrogenation proceeds according to Ping-Pong bi-bi kinetics two-step base-assisted elimination (E2cB)...
Extended synaptotagmins (E-Syts) localize at membrane contact sites between the endoplasmic reticulum (ER) and plasma to mediate inter-membrane lipid transfer control homeostasis. All known E-Syts contain an N-terminal transmembrane (TM) hairpin, a central synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain, three or five C2 domains their C termini. Here we report uncharacterized E-Syt from protist parasite
Celem badania bylo sprawdzenie czy wielkośc źrenic i symetrycznośc twarzy wplyną na zaufanie mierzone wysokością kwot wysylanych w grze ekonomicznej oraz deklaracyjny poziom sympatii zaufania wobec wspolgracza mierzony autorskim kwestionariuszem. Sto czterdzieści cztery kobiety wziely udzial , ktorej manipulowano wielkością symetrycznością zdjeciu mezczyzny. Wbrew przypuszczeniom, zarowno źrenic, jak nie wplynely kwotą wysylaną grze. Wykryto natomiast wplyw deklarowanej kwestionariuszu –...
Extended synaptotagmins (E-Syts) are a group of evolutionarily conserved proteins localizing at membrane contact sites between the endoplasmic reticulum (ER) and plasma membrane, where they mediate inter-membrane lipid transfer control homeostasis. There three E-Syts in mammals, which all contain an N-terminal transmembrane (TM) hairpin for association with ER central synaptotagmin-like mitochondrial-lipid binding protein (SMP) domain as carrier phospholipids. Additionally, mammalian E-Syt1...
3-Ketosteroid Δ1-dehydrogenases (KstD) are important microbial flavin enzymes that initiate the metabolism of steroid ring A and find application in synthesis drugs. We present a structure KstD from Sterolibacterium denitrificans (AcmB), which contains previously uncharacterized putative membrane-associated domain extended proton-relay system. The experimental theoretical studies show 1-dehydrogenation proceeds according to Ping-Pong bi-bi kinetics two-step base-assisted elimination (E2cB)...
Extended synaptotagmins (E-Syts) are a group of evolutionarily conserved proteins localizing at membrane contact sites between the endoplasmic reticulum (ER) and plasma membrane, where they mediate inter-membrane lipid transfer control homeostasis. There three E-Syts in mammals, which all contain an N-terminal transmembrane (TM) hairpin for association with ER central synaptotagmin-like mitochondrial-lipid binding protein (SMP) domain as carrier phospholipids. Additionally, mammalian E-Syt1...
Abstract Background 3-Ketosteroid Δ 1 -dehydrogenases (KSTDs) are the enzymes involved in microbial cholesterol degradation and modification of steroids. They catalyze dehydrogenation between C1 C2 atoms ring A polycyclic structure 3-ketosteroids. KSTDs substrate spectrum is broad, even though most them prefer steroids with small substituents at C17 atom. The investigation KSTD’s specificity hindered by poor solubility hydrophobic aqueous solutions. In this paper, we used...