Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Gerhard Schenk"'
Autor:
Waleed M. Hussein, Luke W. Guddat, Siti Hajar Mohd-Pahmi, Gerhard Schenk, Daniel Feder, Ross P. McGeary
Publikováno v:
ChemMedChem. 16(21)
Metallohydrolases form a large group of enzymes that have fundamental importance in a broad range of biological functions. Among them, the purple acid phosphatases (PAPs) have gained attention due to their crucial role in the acquisition and use of p
Autor:
Filipy Gobbo Maranha, Cláudia Donald Pereira, Nathalia Castilho, Giliandro Farias, Hernán Terenzi, Gerhard Schenk, Rosely A. Peralta, Bernardo de Souza, Ademir Neves
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 24:675-691
In this paper, the catalytic effects of aminoguanidine and aminopurine groups in the second sphere of a FeIIIZnII complex that mimics the active site of the metallohydrolase purple acid phosphatase (PAP) are investigated, with a particular view on DN
Publikováno v:
ChemBioChem. 20:1536-1540
Purple acid phosphatases (PAPs) are members of the large family of metallohydrolases, a group of enzymes that perform a wide range of biological functions, while employing a highly conserved catalytic mechanism. PAPs are found in plants, animals and
Publikováno v:
European Journal of Medicinal Chemistry. 157:462-479
Purple acid phosphatases (PAPs) are metalloenzymes that catalyse the hydrolysis of phosphate esters under acidic conditions. Their active site contains a Fe(III)Fe(II) metal centre in mammals and a Fe(III)Zn(II) or Fe(III)Mn(II) metal centre in plant
Publikováno v:
Journal of Inorganic Biochemistry. 162:343-355
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 pival
Autor:
Robert J Henry, Susanne Schmidt, Luke W. Guddat, Agnelo Furtado, Daniel Feder, Ross P. McGeary, Gerhard Schenk, Nataša Mitić, Benjamin L. Schulz, Thierry G. A. Lonhienne
Phosphate acquisition by plants is an essential process that is directly implicated in the optimization of crop yields. Purple acid phosphatases (PAPs) are ubiquitous metalloenzymes, which catalyze the hydrolysis of a wide range of phosphate esters a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90d8cfe3c574bf74b10a02ff5882e772
Autor:
Daniel Feder, Gerhard Schenk, Luke W. Guddat, Meng-Wei Kan, Ross P. McGeary, Waleed M. Hussein
Publikováno v:
European journal of medicinal chemistry. 182
Purple acid phosphatases (PAPs) are binuclear hydrolases that catalyse the hydrolysis of phosphorylated substrates under acidic to neutral conditions. Elevated serum concentrations of PAP are observed in patients suffering from osteoporosis, identify
Publikováno v:
MedChemComm. 10(1)
Transgenic studies in animals have demonstrated a direct association between the level of expression of purple acid phosphatase (PAP; also known as tartrate-resistant acid phosphatase) and the progression of osteoporosis. Consequently, PAP has emerge
Autor:
Peter Comba, Annie K. Powell, Gerhard Schenk, Simone Bosch, Graeme R. Hanson, Hubert Wadepohl, Paul V. Bernhardt, Lawrence R. Gahan, Valeriu Mereacre, Christopher J. Noble
Publikováno v:
Inorganic Chemistry. 54:7249-7263
The active site of mammalian purple acid phosphatases (PAPs) have a dinuclear iron site in two accessible oxidation states (Fe(III)2 and Fe(III)Fe(II)), and the heterovalent is the active form, involved in the regulation of phosphate and phosphorylat
Publikováno v:
European Journal of Inorganic Chemistry. 2015:3076-3086
Purple acid phosphatases (PAPs) are the only dinuclear metallohydrolases for which the necessity for a heterovalent active site (Fe-III-M-II; M = Fe, Zn or Mn) for catalysis has been established. A major goal for the synthesis of PAP biomimetics is t