Results 261 to 270 of about 850,773 (307)
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Biochemistry, 2002
Cdc25 is a dual-specificity phosphatase that catalyzes the activation of the cyclin-dependent kinases, thus causing initiation and progression of successive phases of the cell cycle. Although it is not significantly homologous in sequence or structure to other dual-specificity phosphatases, Cdc25 belongs to the class of well-studied cysteine ...
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Cdc25 is a dual-specificity phosphatase that catalyzes the activation of the cyclin-dependent kinases, thus causing initiation and progression of successive phases of the cell cycle. Although it is not significantly homologous in sequence or structure to other dual-specificity phosphatases, Cdc25 belongs to the class of well-studied cysteine ...
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Catalytic mechanism of tyrosinases
Tyrosinases (TYR) play a key role in melanin biosynthesis by catalyzing two reactions: monophenolase and diphenolase activities. Despite low amino acid sequence homology, TYRs from various organisms (from bacteria to humans) have similar active site architectures and catalytic mechanisms. The active site of the TYRs contains two copper ions coordinatedSamaneh, Zolghadri, Ali Akbar, Saboury
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Catalytic Reaction Mechanism Testing
Russian Journal of Physical Chemistry B, 2008Experimental tests for determining the mechanism of catalytic reactions were suggested. Quantitative relations were obtained that allowed the mechanism of formation of product molecules in an arbitrary catalytic reaction to be determined by isothermic relaxation methods.
V. F. Kharlamov, F. V. Kharlamov
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Catalytic RNA: Structure and Mechanism
Biochemical Society Transactions, 1993The Hopkins Lecturer is given the charge of explaining how advances in other fields of science have had an impact on his or her own field of biochemistry. A moment’s thought revealed that it was not at all difficult to think of examples where other scientific fields have provided necessary groundwork for the study of RNA catalysis or RNA biochemistry ...
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Enzymes and Catalytic Mechanisms
2007Enzymes catalyze the biochemical reactions in cells of all organisms. These reactions constitute the chemical basis of life. Most enzymes are proteins—a few are ribonucleic acids or ribonucleoproteins—and the catalytic machinery is located in a relatively small active site, where substrates bind and are chemically processed into products. Illustrations
Perry A. Frey, Adrian D. Hegeman
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Aldehyde Dehydrogenase Catalytic Mechanism
1999Elsewhere in this volume we detail findings from an alignment of 145 ALDH sequences (Perozich et al., 1999), and previously at these meetings we reported that the crystal structure of a class 3 ALDH (E-NAD binary complex) revealed a non-traditional mode of NAD-binding within an open β/α domain otherwise familiar in the NAD-binding “ossmann folds” of ...
John Hempel +7 more
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Catalytic mechanism of UDP-glucose dehydrogenase
Biochemical Society Transactions, 2019Abstract UDP-glucose dehydrogenase (UGDH), an oxidoreductase, catalyzes the NAD+-dependent four-electron oxidation of UDP-glucose to UDP-glucuronic acid. The catalytic mechanism of UGDH remains controversial despite extensive investigation and is classified into two types according to whether an aldehyde intermediate is generated in the ...
Jun Chen, Shulin Yang
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The Catalytic Mechanism of Peroxiredoxins
2007Peroxiredoxins carry out the efficient reduction of a typically broad range of peroxide substrates through an absolutely conserved, activated cysteine residue within a highly conserved active site pocket structure. Though details of reductive recycling after cysteine sulfenic acid formation at the active site vary among members of different Prx classes,
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Catalytic Mechanism-based Design
2023In this chapter, carefully selected examples have been elaborated to illustrate how catalytic mechanism-based inhibitors can be elegantly developed for different types of enzymatic reactions involved in various life processes and therapeutic areas. Every effort has been made to ensure an updated and succinct yet comprehensive coverage of the subject ...
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Catalytic Mechanism of Fungal Homoserine Transacetylase
Biochemistry, 2005Homoserine transacetylase is a required catalyst in the biochemical pathway that metabolizes Asp to Met in fungi. The enzyme from the yeast Schizosaccharomyces pombe activates the hydroxyl group of L-homoserine by acetylation from acetyl coenzyme A. This enzyme is unique to fungi and some bacteria and presents an important new target for drug discovery.
Ishac, Nazi, Gerard D, Wright
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