?Peptidatische? Wirksamkeit einer Reihe von Metallionen

Bamann, Eugen; Haas, Johann Georg; Trapmann, Heinz

doi:10.1007/bf00599100

Cited by 6 publications

(4 citation statements)

References 4 publications

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“…Additional, detailed information can be found in a number of excellent and comprehensive review articles written on this subject [60][61][62][99][100][101][102][103][104][105][106][107][108][109][110][111]. More importantly, this paper focuses on recent developments contributing to the design of synthetic metalloproteases that catalyze the hydrolysis of peptide and protein substrates under near physiological conditions of temperature and pH.…”

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confidence: 99%

Major Advances in the Hydrolysis of Peptides and Proteins by Metal Ions and Complexes

Grant¹,

Kassai

2006

COC

116

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Metal ions and complexes that hydrolyze peptides and proteins have become increasingly important in recent years. These reagents have shown great promise for use in a variety of applications including protein sequencing and proteomics. When metal-assisted hydrolytic cleavage is accomplished under nondenaturing conditions of temperature and pH, their use can be extended to include the study of protein function and solution structure, the generation of semisynthetic proteins, the proteolytic cleavage of bioengineered fusion proteins, and therapeutics. Yet, because of the extreme stability of the peptide amide bond, hydrolytically active metals are limited in number and there is now great interest in the development of new, more efficient reagents. In this review, we provide a description of relevant, early work with metal ions and complexes that have been used to hydrolyze unactivated peptide amide bonds in peptides and proteins. More importantly, we present an overview of recent contributions that have been made toward the development of synthetic metalloproteases that catalyze hydrolysis under near physiological conditions of temperature and pH.Dedicated to Professor Koji Nakanishi on the occasion of his 80 th birthday.

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confidence: 99%

Major Advances in the Hydrolysis of Peptides and Proteins by Metal Ions and Complexes

Grant¹,

Kassai

2006

COC

116

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“…Hydrolytic cleavage of biocidic phosphate esters and of nucleic acids is of much current interest, in particular after the re-discovery of highly charged metal cations as effective catalysts . We have directed our efforts in this field mostly toward the development of stable yet active metal complexes and of ligands, which as in related metalloenzymes can further enhance the efficiency of these artificial nucleases, which are still several powers of magnitude below that of natural counterparts.…”

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confidence: 99%

Carboxylic Groups as Cofactors in the Lanthanide-Catalyzed Hydrolysis of Phosphate Esters. Stabilities of Europium(III) Complexes with Aza-benzo-15-crown-5 Ether Derivatives and Their Catalytic Activity vs Bis(p-nitrophenyl)phosphate and DNA

et al. 1999

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The stability of europium(III) complexes with benzocrown ether derivatives 2−4 containing carboxylic functions with methylene spacers of different length was found to vary surprisingly little. In sharp contrast, the hydrolytic activity of these catalysts against bis(p-nitrophenyl)phosphate (BNPP) varied by a factor of 30. The results show for the first time the efficiency of the carboxylic group as cofactor in phosphate ester hydrolysis, which until now was established only in some enzmyes. Other than with BNPP, the hydrolysis with plasmid DNA (nicking experiments) showed no rate enhancement.

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“…Numerous examples of peptide hydrolysis have been achieved with the assistance of metal ions/metal complexes, including Zn, Co, Zr, Cu, Ni, Mo, Pd, and Pt. Detailed information can be found in a number of excellent and comprehensive review articles written on this subject [32][33][34][35][36][37][38][39][40][41][42][43][44][45][46][47][48]. According to the recognition mode, the site-selective peptide/protein degradation can be achieved in two ways: a direct metal-peptide side chain interaction or a promoter's recognition site-peptide side chain interaction.…”

Section: Metal-promoted Peptide Hydrolysis/solvolysismentioning

confidence: 99%