Concise synthesis of sulfoquinovose and sulfoquinovosyl diacylglycerides, and development of a fluorogenic substrate for sulfoquinovosidases

2020 ◽  
Vol 18 (4) ◽  
pp. 675-686
Author(s):  
Yunyang Zhang ◽  
Janice W.-Y. Mui ◽  
Thimali Arumaperuma ◽  
James P. Lingford ◽  
Ethan D. Goddard-Borger ◽  
...  
Keyword(s):  
Efficient Synthesis ◽  
Fluorogenic Substrate ◽  
Sulfoquinovosyl Diacylglycerol ◽  
Kinetic Investigations

A new and efficient synthesis of sulfoquinovose [including (13C6)-SQ] and of saturated and unsaturated sulfoquinovosyl diacylglycerol derivatives, and development of a fluorogenic glycoside useful for kinetic investigations on sulfoquinovosidases.

Synthesis of Sulfoquinovose and Sulfoquinovosyl Diacylglycerides, and a Fluorogenic Substrate for Sulfoquinovosidases

2019 ◽  
Author(s):  
Yunyang Zhang ◽  
Janice Mui ◽  
Thimali Arumaperuma ◽  
James P. Lingford ◽  
ETHAN GODDARD-BORGER ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Fluorogenic Substrate ◽  
Potassium Salts ◽  
X Ray ◽  
Sulfoquinovosyl Diacylglycerol ◽  
Sodium And Potassium

<p>The sulfolipid sulfoquinovosyl diacylglycerol (SQDG) and its headgroup, the sulfosugar sulfoquinovose (SQ), are estimated to harbour up to half of all organosulfur in the biosphere. SQ is liberated from SQDG and related glycosides by the action of sulfoquinovosidases (SQases). We report a 10-step synthesis of SQDG that we apply to the preparation of saturated and unsaturated lipoforms. We also report an expeditious synthesis of SQ and (<sup>13</sup>C<sub>6</sub>)SQ, and X-ray crystal structures of sodium and potassium salts of SQ. Finally, we report the synthesis of a fluorogenic SQase substrate, methylumbelliferyl a-D-sulfoquinovoside, and examination of its cleavage kinetics by two recombinant SQases.</p>

Synthesis of Sulfoquinovose and Sulfoquinovosyl Diacylglycerides, and a Fluorogenic Substrate for Sulfoquinovosidases

2019 ◽  
Author(s):  
Yunyang Zhang ◽  
Janice Mui ◽  
Thimali Arumaperuma ◽  
James P. Lingford ◽  
ETHAN GODDARD-BORGER ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Fluorogenic Substrate ◽  
Potassium Salts ◽  
X Ray ◽  
Sulfoquinovosyl Diacylglycerol ◽  
Sodium And Potassium

<p>The sulfolipid sulfoquinovosyl diacylglycerol (SQDG) and its headgroup, the sulfosugar sulfoquinovose (SQ), are estimated to harbour up to half of all organosulfur in the biosphere. SQ is liberated from SQDG and related glycosides by the action of sulfoquinovosidases (SQases). We report a 10-step synthesis of SQDG that we apply to the preparation of saturated and unsaturated lipoforms. We also report an expeditious synthesis of SQ and (<sup>13</sup>C<sub>6</sub>)SQ, and X-ray crystal structures of sodium and potassium salts of SQ. Finally, we report the synthesis of a fluorogenic SQase substrate, methylumbelliferyl a-D-sulfoquinovoside, and examination of its cleavage kinetics by two recombinant SQases.</p>

A new facile and efficient synthesis of trans-(+)-sobrerol by biotransformation of α-pinene using extremophiles microorganisms

Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
LA Vilaseca ◽  
J Quillaguamán ◽  
L Fuentes ◽  
O Sterner
Keyword(s):  
Efficient Synthesis

Chromatographic Isolation of the LDH-Isoenzymes of Human Blood Platelets and an Investigation of Their Enzyme Kinetics

1968 ◽  
Vol 20 (03/04) ◽  
pp. 301-313 ◽  
Author(s):  
W Schneider ◽  
K Schumacher ◽  
B Thiede ◽  
R Gross
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Deae Cellulose ◽  
Order Reaction ◽  
Kinetic Properties ◽  
Ldh Isoenzymes ◽  
Kinetic Investigations ◽  
Substrate Concentrations ◽  
Chromatographic Isolation ◽  
Human Blood Platelets

SummaryThe LDH-isoenzymes of human blood platelets show a distinct predominance of the isoenzymes 2 and 3 upon chromatography on DEAE-cellulose. Small amounts of LDH-1 are also present, while only traces of LDH-4 and -5 can be detected.Enzyme kinetic investigations of the principal isoenzymes LDH-1, -2 and -3 clearly show that the differences in inhibition constants with pyruvate as substrate which are demonstrable at 25° largely disappear at 37°. On the other hand, the differences among the isoenzymes in their affinity for pyruvate and lactate as substrate as well as in with respect to the optimal substrate concentrations of pyruvate are more marked at 37° than at 25°. Also, the type of inhibition found with lactate as substrate is increasingly the expression of a higher order reaction in going from LDH-1 to LDH-3. A dependence of the LDH distribution pattern upon the metabolism of the cell is discussed. A comparison of our results with thrombocytes with those of other workers with erythrocytes and leucocytes makes it unlikely that the LDH pattern is directly dependent upon the existence of an oxidative metabolism. Rather, the redox potential of the cell could be of importance for the nature of the pattern of isoenzymes and for their differing kinetic properties.

A New Fluorogenic Substrate Method for Assay of Bacterial Endotoxins Using Limulus Hemocyte Lysate

1979 ◽  
Author(s):  
T Harada ◽  
M Ohki ◽  
M Niwa ◽  
S Iwanaga
Keyword(s):  
Antithrombin Iii ◽  
Assay Method ◽  
Sensitive Assay ◽  
Fluorogenic Substrate ◽  
Toxin Concentration ◽  
Amidase Activity ◽  
E Coli ◽  
Bacterial Endotoxins ◽  
Plasmin Inhibitor ◽  
Limulus Test

Limulus hemocyte lysate contains a proclotting enzyme, which is transformed to the active clotting enzyme in the presence of gram-negative bacterial endotoxins. The clotting enzyme coagulates a clottable protein, named coagulogen, contained also in the lysate. This gelation reaction of the lysate, named Limulus test, has been widely employed as a simple and very sensitive assay method for endotoxins. We developed a new fluorogenic substrate, Boc-Leu-Gly-Arg-4-methylcoumarin amide, for Limulus clotting enzyme and established an enzymatic assay method for endotoxins, using the substrate. Because the endotoxin mediates the activation of proclotting enzyme in the lysate, the measurement of amidase activity could be applicable for quantitation of the endotoxins. In fact, the amidase activity determined fluorometrically increased by increasing concentration of E. coli 0111: B4 endotoxin added to the lysate, and a linear relationship between the toxin concentration and the activity was observed in the range of 5X10-6to 5xl0-2 µg endotoxin. The method was a fifty times more sensitive than that of the Limulus test and was very reproducible. However, the method was not directly applicable for the assay of endotoxins in circulating blood, as the amidase activity was strongly inhibited by antithrombin III and α2-plasmin inhibitor. Thus, some pretreatment with heat or chloroform on plasma samples before the assay was required.

Kinetic Investigations of Boronized Cold Work Tool Steels

2014 ◽  
Vol 56 (2) ◽  
pp. 104-110 ◽  
Author(s):  
Polat Topuz ◽  
Eren Yılmaz ◽  
Emine Gündoğdu
Keyword(s):  
Cold Work ◽  
Tool Steels ◽  
Kinetic Investigations

Highly efficient synthesis of methyl ethyl ketone oxime through ammoximation over Ti-MOR catalyst

2014 ◽  
Vol 34 (1) ◽  
pp. 243-250
Author(s):  
Jianghong DING ◽  
Le XU ◽  
Hao XU ◽  
Haihong WU ◽  
Yueming LIU ◽  
...  
Keyword(s):  
Methyl Ethyl Ketone ◽  
Methyl Ethyl ◽  
Efficient Synthesis ◽  
Highly Efficient
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