A Recyclable Hydrophobic Anchor-Tagged Asymmetric Amino Thiourea Catalyst

ChemCatChem ◽  
2018 ◽  
Vol 10 (16) ◽  
pp. 3402-3405 ◽  
Author(s):  
Takahisa Jichu ◽  
Tsubasa Inokuma ◽  
Keisuke Aihara ◽  
Taiki Kohiki ◽  
Kodai Nishida ◽  
...  
Keyword(s):  
Hydrophobic Anchor

Synthesis of the Antimalarial Peptide Aldehyde, a Precursor of Kozupeptin A, Utilizing a Designed Hydrophobic Anchor Molecule

2019 ◽  
Vol 21 (20) ◽  
pp. 8229-8233 ◽  
Author(s):  
Yumi Hayashi ◽  
Tomoyasu Hirose ◽  
Masato Iwatsuki ◽  
Satoshi O̅mura ◽  
Toshiaki Sunazuka
Keyword(s):  
Hydrophobic Anchor

scholarly journals The characterization and interconversion of three forms of cholesterol oxidase extracted from Nocardia rhodochrous

1982 ◽  
Vol 201 (3) ◽  
pp. 515-521 ◽  
Author(s):  
P S J Cheetham ◽  
P Dunnill ◽  
M D Lilly
Keyword(s):  
Cell Membrane ◽  
Membrane Lipids ◽  
Cholesterol Oxidase ◽  
Hydrophobic Region ◽  
Hydrophobic Domain ◽  
Solubilized Enzyme ◽  
High Concentrations ◽  
Triton X ◽  
Catalytic Functions ◽  
Hydrophobic Anchor

The physical properties and the methods used for interconversion of three forms of cholesterol oxidase extracted from Nocardia rhodochrous by treatment with Triton X-100, trypsin or buffer alone provide evidence that these forms differ chiefly in the possession or absence of a hydrophobic anchor region connected by a trypsin-sensitive region. The hydrophobic domain normally integrates the enzyme into the cell membrane and confers amphipathic properties on the solubilized enzyme, causing adsorption to hydrophobic resins, aggregation when detergent is removed and formation of mixed micelles with detergent and cholesterol resulting in surface-dilution kinetic behaviour and activation by relatively high concentrations of water-miscible solvents. By contrast, only the enzymic fragment is extracted with trypsin and it behaves as a conventional soluble enzyme and does not aggregate or interact with hydrophobic resins, detergents or water-miscible solvents. As no phospholipid could be detected in the enzyme extracts, the detergent appears to act as a substitute for the cell-membrane lipids that would normally interact with the hydrophobic region. This cholesterol oxidase is an example of a prokaryotic enzyme possessing two closely associated catalytic functions, dehydrogenase and isomerase activities, and an anchoring function.

The hydrophobic anchor of small-intestinal sucrase-isomaltase

FEBS Letters ◽  
1978 ◽  
Vol 96 (1) ◽  
pp. 183-188 ◽  
Author(s):  
Gerhard Frank ◽  
Joseph Brunner ◽  
Helmut Hauser ◽  
Hans Wacker ◽  
Giorgio Semenza ◽  
...  
Keyword(s):  
Small Intestinal ◽  
Intestinal Sucrase ◽  
Hydrophobic Anchor

scholarly journals Membrane Topography of the Hydrophobic Anchor Sequence of Poliovirus 3A and 3AB Proteins and the Functional Effect of 3A/3AB Membrane Association upon RNA Replication†

Biochemistry ◽  
2007 ◽  
Vol 46 (17) ◽  
pp. 5185-5199 ◽  
Author(s):  
Kentaro Fujita ◽  
Shyam S. Krishnakumar ◽  
David Franco ◽  
Aniko V. Paul ◽  
Erwin London ◽  
...  
Keyword(s):  
Rna Replication ◽  
Membrane Association ◽  
Functional Effect ◽  
Membrane Topography ◽  
Anchor Sequence ◽  
Hydrophobic Anchor

Decorated reduced graphene oxide for photo-chemotherapy

2016 ◽  
Vol 4 (5) ◽  
pp. 929-937 ◽  
Author(s):  
Yanfang Hu ◽  
Diankui Sun ◽  
Jianxun Ding ◽  
Li Chen ◽  
Xuesi Chen
Keyword(s):  
Surface Modification ◽  
Graphene Oxide ◽  
Reduced Graphene Oxide ◽  
Reduced Graphene ◽  
Hydrophobic Anchor

A novel surface modification strategy to prepare dextran decorated reduced graphene oxide (rGO) sheets for photo-chemotherapy has been presented. In this strategy, octadecanic acid is conjugated on dextran and used as a hydrophobic anchor to prepare dextran decorated rGO sheets.

scholarly journals The N-terminal amino acid sequence of pig kidney endopeptidase-24.11 shows homology with pro-sucrase-isomaltase

1986 ◽  
Vol 240 (1) ◽  
pp. 305-308 ◽  
Author(s):  
I S Fulcher ◽  
D J Pappin ◽  
A J Kenny
Keyword(s):  
Amino Acid ◽  
Solid Phase ◽  
Consensus Sequence ◽  
Terminal Segment ◽  
Amino Acid Residues ◽  
Endopeptidase 24.11 ◽  
Cytoplasmic Face ◽  
Arginine Residues ◽  
Terminal Amino ◽  
Hydrophobic Anchor

Endopeptidase-24.11 (EC 3.4.24.11), a widely distributed ectoenzyme, was isolated from pig kidneys by detergent solubilization of membranes and immuno-affinity chromatography. In all, 12 preparations of the enzyme were submitted to solid-phase sequencing, yielding a consensus sequence of 25 amino acid residues of the N-terminal segment. Some samples were treated with either trypsin or Staphylococcus aureus V8 proteinase before sequencing. There were four lysine and one arginine residues in the first nine positions. This segment was susceptible to hydrolysis by trypsin and, in some samples, to endogenous proteinases. From residue 19 onwards, the sequence became intensely hydrophobic. There was a striking homology with the N-terminal sequence of pro-sucrase-isomaltase. From Lys7 to Leu20 there were seven identical amino acid residues and four conservative substitutions. We suggest that endopeptidase-24.11 is topologically similar to this glycosidase, the N-terminus at the cytoplasmic face and hydrophobic segment serving the roles of both signal peptide and hydrophobic anchor.

Tryptophan oxygenation: mechanistic considerations

2012 ◽  
Vol 40 (3) ◽  
pp. 509-514 ◽  
Author(s):  
James H. Naismith
Keyword(s):  
Natural Products ◽  
Amino Acid ◽  
Molecular Oxygen ◽  
Ring System ◽  
Hydrophobic Core ◽  
Indole Ring ◽  
Multiple Strategies ◽  
Tryptophan Dioxygenase ◽  
Recent Developments ◽  
Hydrophobic Anchor

From a protein structural viewpoint, tryptophan is often considered an inert structural amino acid, playing a role as a hydrophobic anchor in membrane proteins or as part of the hydrophobic core of soluble proteins. However, tryptophan is the only polyaromatic amino acid and, from a chemical viewpoint, possesses unique reactivity owing to the electron-richness of the indole system. This reactivity is seen in the area of natural products and metabolites which have exquisite modifications of the indole ring system. Enzymes have evolved multiple strategies to break or modify the indole ring; one particular class is the IDO/TDO (indoleamine/tryptophan dioxygenase) superfamily. A new member of this family, PrnB, on the surface catalyses a very different reaction, but actually shares much of the early chemistry with the tryptophan dioxygenases. Studies on PrnB have contributed to our understanding of the wider superfamily. In the present mini-review, recent developments in our understanding of how the TDO class of enzymes use activated molecular oxygen to break the indole ring are discussed.

scholarly journals Phosphatidylinositol may serve as the hydrophobic anchor for immobilization of proteins on liposome surface

FEBS Letters ◽  
1982 ◽  
Vol 138 (1) ◽  
pp. 117-120 ◽  
Author(s):  
V.P. Torchilin ◽  
A.L. Klibanov ◽  
V.N. Smirnov
Keyword(s):  
Liposome Surface ◽  
Hydrophobic Anchor
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