The role of the carbonyl group in the intermolecular 1,3-cycloaddition of azido(2-heteroaryl)methanones with activated olefins

2002 ◽  
pp. 1420-1425 ◽  
Author(s):  
Paolo Zanirato
Keyword(s):  
Carbonyl Group ◽  
Activated Olefins

Role of the carbonyl group of local anesthetics in their anesthetic effect

1972 ◽  
Vol 73 (5) ◽  
pp. 553-556
Author(s):  
V. M. Belobrov ◽  
I. V. Komissarov ◽  
L. E. Makarova ◽  
N. Z. Rudenko ◽  
E. V. Titov
Keyword(s):  
Carbonyl Group ◽  
Local Anesthetics ◽  
Anesthetic Effect

Structure of a proteolytically resistant analogue of (NLys)5SFTI-1 in complex with trypsin: evidence for the direct participation of the Ser214 carbonyl group in serine protease-mediated proteolysis

2014 ◽  
Vol 70 (3) ◽  
pp. 668-675 ◽  
Author(s):  
Szymon Krzywda ◽  
Mariusz Jaskolski ◽  
Krzysztof Rolka ◽  
Maciej J. Stawikowski
Keyword(s):  
Hydrogen Bond ◽  
Carbonyl Group ◽  
Serine Proteases ◽  
Peptide Ligands ◽  
Protein Protein Interaction ◽  
Proteolytic Resistance ◽  
Structural Differences ◽  
Natural Inhibitor ◽  
Insight Into

Peptide–peptoid hybrids are found to be potent inhibitors of serine proteases. These engineered peptidomimetics benefit from both types of units of the biopolymeric structure: the natural inhibitor part serves as a good binding template, while the P1-positioned peptoid component provides complete resistance towards proteolysis. In this report, the mechanism of proteolytic resistance of a P1 peptoid-containing analogue is postulated based on the crystal structure of the (NLys)5-modified sunflower trypsin inhibitor SFTI-1 in complex with bovine trypsin solved at 1.29 Å resolution. The structural differences between the (NLys)5SFTI-1–trypsin complex and the native SFTI-1–trypsin complex are surprisingly small and reveal the key role of the carbonyl group of the Ser214 residue of the enzyme, which is crucial for binding of the inhibitor and plays a crucial role in proteolysis mediated by serine proteases. The incorporatedNLys5 peptoid residue prevents Ser214 from forming a hydrogen bond to the P1 residue, and in turn Gln192 does not form a hydrogen bond to the carbonyl group of the P2 residue. It also increases the distance between the Ser214 carbonyl group and the Ser195 residue, thus preventing proteolysis. The hybrid inhibitor structure reported here provides insight into protein–protein interaction, which can be efficiently and selectively probed with the use of peptoids incorporated within endogenous peptide ligands.

Role of the Carbonyl Group in Thioester Chain Length Recognition by the Medium Chain Acyl-CoA Dehydrogenase

Biochemistry ◽  
1995 ◽  
Vol 34 (27) ◽  
pp. 8597-8605 ◽  
Author(s):  
Raymond C. Trievel ◽  
Rong Wang ◽  
Vernon E. Anderson ◽  
Colin Thorpe
Keyword(s):  
Carbonyl Group ◽  
Chain Length ◽  
Medium Chain ◽  
Chain Acyl

Chemoselective acyl C–O bond activation in esters for Suzuki–Miyaura coupling

2017 ◽  
Vol 4 (7) ◽  
pp. 1430-1434 ◽  
Author(s):  
Manoj Mondal ◽  
Tahshina Begum ◽  
Utpal Bora
Keyword(s):  
Carbonyl Group ◽  
Bond Activation ◽  
Oxidative Addition ◽  
Mechanistic Studies

The use of palladium–NHC (bulky) catalyst enables selective acylative coupling in esters via blocking the potential C(aryl)–O oxidative addition and decarbonylation processes. Mechanistic studies elucidate the role of bulky carbene catalysts in promoting C(acyl)–O activation, and as a result, the acyl metal intermediates undergo coupling without the loss of carbonyl group.

The role of S-bond in tenoxicam keto–enolic tautomerization

CrystEngComm ◽  
2019 ◽  
Vol 21 (36) ◽  
pp. 5392-5401 ◽  
Author(s):  
Sergey G. Arkhipov ◽  
Peter S. Sherin ◽  
Alexey S. Kiryutin ◽  
Vladimir A. Lazarenko ◽  
Christian Tantardini
Keyword(s):  
Carbonyl Group ◽  
Crucial Role ◽  
Sulphur Atom ◽  
Covalent Interaction

A non-covalent interaction between the sulphur atom of thiophenyl moiety and oxygen of the carbonyl group (S-bond) plays a crucial role in keto–enol tautomerization of tenoxicam leading to the crystallization of latter only in zwitterionic (ZWC) and not in β-keto–enolic (BKE) form.

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