Search results for: Gerhard Schenk

Items from 1 to 20 out of 103 results

article

Structural and Functional Insight into the Mechanism of the Fe−S Cluster‐Dependent Dehydratase from Paralcaligenes ureilyticus

Tenuun Bayaraa, Thierry Lonhienne, Samuel Sutiono, Okke Melse, more

Chemistry – A European Journal > 29 > 9 > n/a - n/a

Enzyme‐catalyzed reaction cascades play an increasingly important role for the sustainable manufacture of diverse chemicals from renewable feedstocks. For instance, dehydratases from the ilvD/EDD superfamily have been embedded into a cascade to convert glucose via pyruvate to isobutanol, a platform chemical for the production of aviation fuels and other valuable materials. These dehydratases depend...

article

Molecular characterization of cyanobacterial short‐chain prenyltransferases and discovery of a novel GGPP phosphatase

Alessandro Satta, Lygie Esquirol, Birgitta E. Ebert, Janet Newman, more

The FEBS Journal > 289 > 21 > 6672 - 6693

Cyanobacteria are photosynthetic prokaryotes with strong potential to be used for industrial terpenoid production. However, the key enzymes forming the principal terpenoid building blocks, called short‐chain prenyltransferases (SPTs), are insufficiently characterized. Here, we examined SPTs in the model cyanobacteria Synechococcus elongatus sp. PCC 7942 and Synechocystis sp. PCC 6803. Each species...

article

Dihydroxy‐Acid Dehydratases From Pathogenic Bacteria: Emerging Drug Targets to Combat Antibiotic Resistance

Tenuun Bayaraa, Jose Gaete, Samuel Sutiono, Julia Kurz, more

Chemistry – A European Journal > 28 > 44 > n/a - n/a

There is an urgent global need for the development of novel therapeutics to combat the rise of various antibiotic‐resistant superbugs. Enzymes of the branched‐chain amino acid (BCAA) biosynthesis pathway are an attractive target for novel anti‐microbial drug development. Dihydroxy‐acid dehydratase (DHAD) is the third enzyme in the BCAA biosynthesis pathway. It relies on an Fe−S cluster for catalytic...

article

Discovery of a Pyrimidinedione Derivative with Potent Inhibitory Activity against Mycobacterium tuberculosis Ketol–Acid Reductoisomerase

Xin Lin, Julia L. Kurz, Khushboo M. Patel, Shun Jie Wun, more

Chemistry – A European Journal > 27 > 9 > 3130 - 3141

New drugs aimed at novel targets are urgently needed to combat the increasing rate of drug‐resistant tuberculosis (TB). Herein, the National Cancer Institute Developmental Therapeutic Program (NCI‐DTP) chemical library was screened against a promising new target, ketol–acid reductoisomerase (KARI), the second enzyme in the branched‐chain amino acid (BCAA) biosynthesis pathway. From this library, 6‐hydroxy‐2‐methylthiazolo[4,5‐...

article

Recent Advances in Heterogeneous Catalytic Systems Containing Metal Ions for Phosphate Ester Hydrolysis

Marco Antônio G. B. Gomes, Christiane Fernandes, Lawrence R. Gahan, Gerhard Schenk, more

Chemistry – A European Journal > 27 > 3 > 877 - 887

Organophosphates are a class of organic compounds that are important for living organisms, forming the building blocks for DNA, RNA, and some essential cofactors. Furthermore, non‐natural organophosphates are widely used in industrial applications, including as pesticides; in laundry detergents; and, unfortunately, as chemical weapons agents. In some cases, the natural degradation of organophosphates...

article

Discovery, Synthesis and Evaluation of a Ketol‐Acid Reductoisomerase Inhibitor

Tenuun Bayaraa, Julia L. Kurz, Khushboo M. Patel, Waleed M. Hussein, more

Chemistry – A European Journal > 26 > 41 > 8958 - 8968

Ketol‐acid reductoisomerase (KARI), the second enzyme in the branched‐chain amino acid biosynthesis pathway, is a potential drug target for bacterial infections including Mycobacterium tuberculosis. Here, we have screened the Medicines for Malaria Venture Pathogen Box against purified M. tuberculosis (Mt) KARI and identified two compounds that have K_i values below 200 nm. In Mt cell susceptibility...

article

Guanidine- and purine-functionalized ligands of Fe^IIIZn^II complexes: effects on the hydrolysis of DNA

Claudia Pereira, Giliandro Farias, Filipy G. Maranha, Nathalia Castilho, more

JBIC Journal of Biological Inorganic Chemistry > 2019 > 24 > 5 > 675-691

In this paper, the catalytic effects of aminoguanidine and aminopurine groups in the second sphere of a Fe^IIIZn^II complex that mimics the active site of the metallohydrolase purple acid phosphatase (PAP) are investigated, with a particular view on DNA as substrate. The ligand 3-(((3-((bis(2-(pyridin-2-yl)ethyl)amino)methyl)-2-hydroxy-5-methylbenzyl)(pyridin-2-ylmethyl)amino)meth-yl)-2 hydroxy-5-methylbenzaldehyde—(H...

article

Metabolic strategies for the degradation of the neuromodulator agmatine in mammals

José Benítez, David García, Nicol Romero, Arlette González, more

Metabolism > 2018 > 81 > C > 35-44

Agmatine (1-amino-4-guanidinobutane), a precursor for polyamine biosynthesis, has been identified as an important neuromodulator with anticonvulsant, antineurotoxic and antidepressant actions in the brain. In this context it has emerged as an important mediator of addiction/satiety pathways associated with alcohol misuse. Consequently, the regulation of the activity of key enzymes in agmatine metabolism...

article

Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase from Bacillus subtilis BS-5 with potential applications in the saccharification of cellulosic substrates

Bin Wu, Shan Zheng, Marcelo Monteiro Pedroso, Luke W. Guddat, more

Biotechnology for Biofuels > 2018 > 11 > 1 > 1-15

Background Presently, enzymes still constitute a major part of the cost of biofuel production from lignocellulosic biomass. Processive endoglucanases, which possess both endoglucanase and exoglucanase activity, have the potential to reduce the costs of biomass saccharification when used together with commercial cellulases. Therefore, the exploration of new processive endoglucanases has attracted much...

article

Crystal Structures of Staphylococcus aureus Ketol‐Acid Reductoisomerase in Complex with Two Transition State Analogues that Have Biocidal Activity

Khushboo M. Patel, David Teran, Shan Zheng, Ajit Kandale, more

Chemistry – A European Journal > 23 > 72 > 18289 - 18295

Ketol‐acid reductoisomerase (KARI) is an NAD(P)H and Mg²⁺‐dependent enzyme of the branched‐chain amino acid (BCAA) biosynthesis pathway. Here, the first crystal structures of Staphylococcus aureus (Sa) KARI in complex with two transition state analogues, cyclopropane‐1,1‐dicarboxylate (CPD) and N‐isopropyloxalyl hydroxamate (IpOHA) are reported. These compounds bind competitively and in multi‐dentate...

article

Deacidification of grass silage press juice by continuous production of acetoin from its lactate via an immobilized enzymatic reaction cascade

Hendrik Hohagen, Dominik Schwarz, Gerhard Schenk, Luke W. Guddat, more

Bioresource Technology > 2017 > 245 > PA > 1084-1092

An immobilized enzymatic reaction cascade was designed and optimized for the deacidification of grass silage press juice (SPJ), thus facilitating the production of bio-based chemicals. The cascade involves a three-step process using four enzymes immobilized in a Ca-alginate gel and uses lactic acid to form acetoin, a value-added product. The reaction is performed with a continuous, pH-dependent substrate...

article

High resolution crystal structure of a fluoride-inhibited organophosphate-degrading metallohydrolase

Christopher Selleck, Luke W. Guddat, David L. Ollis, Gerhard Schenk, more

Journal of Inorganic Biochemistry > 2017 > 177 > C > 287-290

Metal ion-dependent, organophosphate-degrading enzymes (OP hydrolases) have received increasing attention due to their ability to degrade and thus detoxify commonly used pesticides and nerve agents such as sarin and VX. These enzymes thus garner strong potential as bioremediators. The OP hydrolase from Agrobacterium radiobacter (OpdA) is one of the most efficient members of this group of enzymes....

article

Structure-activity relationship study and optimisation of 2-aminopyrrole-1-benzyl-4,5-diphenyl-1H-pyrrole-3-carbonitrile as a broad spectrum metallo-β-lactamase inhibitor

Ross P. McGeary, Daniel T.C. Tan, Christopher Selleck, Marcelo Monteiro Pedroso, more

European Journal of Medicinal Chemistry > 2017 > 137 > C > 351-364

A SAR study on derivatives of 2-amino-1-benzyl-4,5-diphenyl-1H-pyrrole-3-carbonitrile 5a revealed that the 3-carbonitrile group, vicinal 4,5-diphenyl and N-benzyl side chains of the pyrrole are important for the inhibitory potencies of these compounds against members representing the three main subclasses of metallo-β-lactamases (MBLs), i.e. IMP-1 (representing the B1 subgroup), CphA (B2) and AIM-1...

article

Is Cu^II Coordinated to Patellamides inside Prochloron Cells?

Peter Comba, Annika Eisenschmidt, Lawrence R. Gahan, Dirk‐Peter Herten, more

Chemistry – A European Journal > 23 > 50 > 12264 - 12274

Dinuclear Cu^II–patellamide complexes (patellamides are naturally occurring cyclic pseudo‐octapeptides) are known to be efficient catalysts for hydrolysis reactions of biological importance, for example, those of phosphatase, carbonic anhydrase, and glycosidase. However, the biological role of patellamides is still unknown. Patellamides were originally extracted from the sea squirt Lissoclinum patella...

article

Visualization of the Reaction Trajectory and Transition State in a Hydrolytic Reaction Catalyzed by a Metalloenzyme

Christopher Selleck, Daniel Clayton, Lawrence R. Gahan, Nataša Mitić, more

Chemistry – A European Journal > 23 > 20 > 4778 - 4781

Metallohydrolases are a vast family of enzymes that play crucial roles in numerous metabolic pathways. Several members have emerged as targets for chemotherapeutics. Knowledge about their reaction mechanisms and associated transition states greatly aids the design of potent and highly specific drug leads. By using a high‐resolution crystal structure, we have probed the trajectory of the reaction catalyzed...

article

Enhancement of antibiotic-activity through complexation with metal ions - Combined ITC, NMR, enzymatic and biological studies

Jasper S. Möhler, Theresa Kolmar, Kevin Synnatschke, Marcel Hergert, more

Journal of Inorganic Biochemistry > 2017 > 167 > C > 134-141

Alternative solutions need to be developed to overcome the growing problem of multi-drug resistant bacteria. This study explored the possibility of creating complexes of antibiotics with metal ions, thereby increasing their activity. Analytical techniques such as isothermal titration calorimetry and nuclear magnetic resonance were used to examine the structure and interactions between Cu(II), Ag(I)...

article

Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases

Nicol Romero, José Benítez, David Garcia, Arlette González, more

Journal of Inorganic Biochemistry > 2017 > 166 > C > 122-125

Agmatine (1-amino-4-guanidinobutane) plays an important role in a range of metabolic functions, in particular in the brain. Agmatinases (AGMs) are enzymes capable of converting agmatine to the polyamine putrescine and urea. AGMs belong to the family of Mn²⁺-dependent ureahydrolases. However, no AGM from a mammalian source has yet been extracted in catalytically active form. While in human AGM the...

article

AIM‐1: An Antibiotic‐Degrading Metallohydrolase That Displays Mechanistic Flexibility

Christopher Selleck, James A. Larrabee, Jeffrey Harmer, Luke W. Guddat, more

Chemistry – A European Journal > 22 > 49 > 17704 - 17714

Antibiotic resistance has emerged as a major threat to global health care. This is largely due to the fact that many pathogens have developed strategies to acquire resistance to antibiotics. Metallo‐β‐lactamases (MBL) have evolved to inactivate most of the commonly used β‐lactam antibiotics. AIM‐1 is one of only a few MBLs from the B3 subgroup that is encoded on a mobile genetic element in a major...

article

Asymmetric mono- and dinuclear GaIII and ZnII complexes as models for purple acid phosphatases

Simone Bosch, Peter Comba, Lawrence R. Gahan, Gerhard Schenk

Journal of Inorganic Biochemistry > 2016 > 162 > C > 343-355

Derivatives of the known dinucleating ligands HL¹ (2,6-bis{[bis(pyridin-2-ylmethyl)amino]methyl}-4-methylphenol) and H₂L² (2-{[bis(pyridin-2-ylmethyl)amino]methyl}-6-{[(2-hydroxybenzyl)(pyridine-2-ylmethyl)amino]methyl}-4-methylphenol) with two pivaloylamido hydrogen bond donor substituents, H₃L³ and H₃L⁵, have been prepared. The mono-, homo- and heterodinuclear Zn^II and Ga^III complexes of these ligands...

article

Preface

Lawrence Gahan, Peter Comba, Gerhard Schenk, Lena Daumann, more

Journal of Inorganic Biochemistry > 2016 > 162 > C > 162-163

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PURPLE ACID PHOSPHATASE (11)
BINUCLEAR METALLOHYDROLASES (10)
ANTIBIOTIC RESISTANCE (8)
BIOMIMETICS (7)
BIOREMEDIATION (6)
METALLOENZYMES (6)
OSTEOPOROSIS (6)
REACTION MECHANISM (6)
ENZYMES (5)
METALLO-Β-LACTAMASE (5)
CATALYSIS (4)
INHIBITION ASSAYS (4)
MAGNETIC CIRCULAR DICHROISM (4)
ANTIBIOTICS RESISTANCE (3)
BRANCHED-CHAIN AMINO ACID BIOSYNTHESIS (3)
CATALYTIC MECHANISM (3)
DINUCLEAR METALLOHYDROLASES (3)
ENZYME CATALYSIS (3)
ENZYME MODELS (3)
KETOL–ACID REDUCTOISOMERASE (3)
METALLO-Β-LACTAMASES (3)
METALLOHYDROLASES (3)
METALLO‐Β‐LACTAMASES (3)
ORGANOPHOSPHATE-DEGRADING ENZYMES (3)
X-RAY CRYSTALLOGRAPHY (3)
AGMATINASE (2)
AGMATINE (2)
BIOINORGANIC CHEMISTRY (2)
CRYSTAL STRUCTURE (2)
CYANOBACTERIA (2)
DNA CLEAVAGE (2)
DRUG DESIGN (2)
DRUG DISCOVERY (2)
ENZYME IMMOBILIZATION (2)
EPR (2)
FE−S CLUSTER (2)
FLUORIDE INHIBITION (2)
HYDROLYSIS (2)
KINETICS (2)
MAGNESIUM (2)
METAL ION REPLACEMENT (2)
METAL IONS (2)
METALLOENZYME (2)
ORGANOPHOSPHATE PESTICIDES (2)
PAP (2)
PHOSPHONATE (2)
PURPLE ACID PHOSPHATASES (2)
PYRROLE (2)
TUBERCULOSIS (2)
UTEROFERRIN (2)
Β-LACTAM ANTIBIOTICS (2)
71GA NMR (1)
3-MERCAPTO-1,2,4-TRIAZOLES (1)
31P NMR (1)
ACID PHOSPHATASE; BINUCLEAR METALLOENZYME; PURPLE ACID PHOSPHATASE; SWEET POTATO; SOYBEAN (1)
AGMATINASE LIKE PROTEIN (1)
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INFONA - science communication portal

Search results for: Gerhard Schenk

Structural and Functional Insight into the Mechanism of the Fe−S Cluster‐Dependent Dehydratase from Paralcaligenes ureilyticus

Molecular characterization of cyanobacterial short‐chain prenyltransferases and discovery of a novel GGPP phosphatase

Dihydroxy‐Acid Dehydratases From Pathogenic Bacteria: Emerging Drug Targets to Combat Antibiotic Resistance

Discovery of a Pyrimidinedione Derivative with Potent Inhibitory Activity against Mycobacterium tuberculosis Ketol–Acid Reductoisomerase

Recent Advances in Heterogeneous Catalytic Systems Containing Metal Ions for Phosphate Ester Hydrolysis

Discovery, Synthesis and Evaluation of a Ketol‐Acid Reductoisomerase Inhibitor

Guanidine- and purine-functionalized ligands of Fe^IIIZn^II complexes: effects on the hydrolysis of DNA

Metabolic strategies for the degradation of the neuromodulator agmatine in mammals

Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase from Bacillus subtilis BS-5 with potential applications in the saccharification of cellulosic substrates

Crystal Structures of Staphylococcus aureus Ketol‐Acid Reductoisomerase in Complex with Two Transition State Analogues that Have Biocidal Activity

Deacidification of grass silage press juice by continuous production of acetoin from its lactate via an immobilized enzymatic reaction cascade

High resolution crystal structure of a fluoride-inhibited organophosphate-degrading metallohydrolase

Structure-activity relationship study and optimisation of 2-aminopyrrole-1-benzyl-4,5-diphenyl-1H-pyrrole-3-carbonitrile as a broad spectrum metallo-β-lactamase inhibitor

Is Cu^II Coordinated to Patellamides inside Prochloron Cells?

Visualization of the Reaction Trajectory and Transition State in a Hydrolytic Reaction Catalyzed by a Metalloenzyme

Enhancement of antibiotic-activity through complexation with metal ions - Combined ITC, NMR, enzymatic and biological studies

Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases

AIM‐1: An Antibiotic‐Degrading Metallohydrolase That Displays Mechanistic Flexibility

Asymmetric mono- and dinuclear GaIII and ZnII complexes as models for purple acid phosphatases

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