scholarly journals Acyl-chain specificity of human milk bile-salt-activated lipase

1991 ◽  
Vol 279 (1) ◽  
pp. 297-302 ◽  
Author(s):  
C S Wang
Keyword(s):  
Human Milk ◽  
Bile Salt ◽  
Chain Length ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Acyl Chain Length ◽  
Enzyme Substrate ◽  
Consistent Trend ◽  
Kinetics Of ◽  
Long Chain

In order to probe the active-site structure of human milk bile-salt-activated lipase (BAL), the kinetics of the BAL-catalysed reaction were studied using monoesters as substrates. Among the fatty acyl chains, ranging from C8 to C16 of monoacylglycerols in a single equimolar assay mixture, there was a consistent trend of increased reactivity with decreased fatty-acyl-chain length for both the basal and taurocholate-stimulated activities of BAL. In addition, the detection of hydrolysis of long-chain monoacylglycerols in the absence of bile salt indicates that it is possible for the long-chain fatty acid monoester to form an enzyme-substrate complex with the basal form of BAL. I further examined the reaction kinetics of BAL with water-soluble short-chain esters of p-nitrophenol. The results indicated that there is a consistent trend towards a decreased Michaelis-Menten constant with increased acyl-chain length. Therefore it was concluded that the decreased reactivity with increased acyl-chain length of acylglycerols is probably not a consequence of the lowered affinity of the substrate for the enzyme. The fact that butyrate ester has the optimum acyl chain to be a substrate of BAL can be attributed to its acyl-chain length being long enough for interaction with the active centre of BAL and short enough to provide adequate positioning of the ester bond for transition state complex formation. The calculated free energy of BAL catalysis based on the derived kinetic parameters provides additional insight into the effect on the enzyme-substrate interaction of increasing the number of methylene groups in the acyl chain of substrates.

Effect of Acylglycerol Composition and Fatty Acyl Chain Length on Lipid Digestion in pH-Stat Digestion Model and SimulatedIn VitroDigestion Model

2015 ◽  
Vol 81 (2) ◽  
pp. C317-C323
Author(s):  
Jin F. Qi ◽  
Cai H. Jia ◽  
Jung A. Shin ◽  
Jeong M. Woo ◽  
Xiang Y. Wang ◽  
...  
Keyword(s):  
Chain Length ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Lipid Digestion ◽  
Acyl Chain Length ◽  
Ph Stat

Lipid profiling of human diabetic myocardium reveals differences in triglyceride fatty acyl chain length and degree of saturation

2020 ◽  
Vol 320 ◽  
pp. 106-111
Author(s):  
Elias Björnson ◽  
Ylva Östlund ◽  
Marcus Ståhlman ◽  
Martin Adiels ◽  
Elmir Omerovic ◽  
...  
Keyword(s):  
Chain Length ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Degree Of Saturation ◽  
Fatty Acyl Chain ◽  
Lipid Profiling ◽  
Acyl Chain Length ◽  
Diabetic Myocardium

The effect of altered sphingolipid acyl chain length on various disease models

2015 ◽  
Vol 396 (6-7) ◽  
pp. 693-705 ◽  
Author(s):  
Woo-Jae Park ◽  
Joo-Won Park
Keyword(s):  
Chain Length ◽  
De Novo ◽  
Case Reports ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Sphingolipid Metabolism ◽  
Lipid Mediator ◽  
Disease Models ◽  
Acyl Chain Length ◽  
Sphingosine 1 Phosphate

Abstract Sphingolipids have emerged as an important lipid mediator in intracellular signalling and metabolism. Ceramide, which is central to sphingolipid metabolism, is generated either via a de novo pathway, by attaching fatty acyl CoA to a long-chain base, or via a salvage pathway, by degrading pre-existing sphingolipids. As a ‘sphingolipid rheostat’ has been proposed, the balance between ceramide and sphingosine-1-phosphate has been the object of considerable attention. Ceramide has recently been reported to have a different function depending on its acyl chain length: six ceramide synthases (CerS) determine the specific ceramide acyl chain length in mammals. All CerS-deficient mice generated to date show that sphingolipids with defined acyl chain lengths play distinct pathophysiological roles in disease models. This review describes recent advances in understanding the associations of CerS with various diseases and includes clinical case reports.

scholarly journals Dependence of fatty acyl chain length on the property of phase separation of GM3/DPPC multilamellar vesicles

2001 ◽  
Vol 41 (supplement) ◽  
pp. S128
Author(s):  
S. Matsuoka ◽  
M. Akiyama ◽  
H. Yamada ◽  
K. Tsuchihashi ◽  
S. Gasa
Keyword(s):  
Phase Separation ◽  
Chain Length ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Multilamellar Vesicles ◽  
Acyl Chain Length

Ketoacyl synthase domain is a major determinant for fatty acyl chain length in Saccharomyces cerevisiae

2013 ◽  
Vol 195 (12) ◽  
pp. 843-852 ◽  
Author(s):  
Juthaporn Sangwallek ◽  
Yoshinobu Kaneko ◽  
Minetaka Sugiyama ◽  
Hisayo Ono ◽  
Takeshi Bamba ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Chain Length ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Major Determinant ◽  
Fatty Acyl Chain ◽  
Acyl Chain Length ◽  
Ketoacyl Synthase

scholarly journals Endocytic Trafficking of Sphingomyelin Depends on Its Acyl Chain Length

2007 ◽  
Vol 18 (12) ◽  
pp. 5113-5123 ◽  
Author(s):  
Mirkka Koivusalo ◽  
Maurice Jansen ◽  
Pentti Somerharju ◽  
Elina Ikonen
Keyword(s):  
Plasma Membrane ◽  
Chain Length ◽  
Human Fibroblasts ◽  
Acyl Chain ◽  
Endocytic Trafficking ◽  
Dependent Manner ◽  
Lipid Trafficking ◽  
Acyl Chain Length ◽  
Escrt Complex ◽  
Long Chain

To study the principles of endocytic lipid trafficking, we introduced pyrene sphingomyelins (PyrSMs) with varying acyl chain lengths and domain partitioning properties into human fibroblasts or HeLa cells. We found that a long-chain, ordered-domain preferring PyrSM was targeted Hrs and Tsg101 dependently to late endosomal compartments and recycled to the plasma membrane in an NPC1- and cholesterol-dependent manner. A short-chain, disordered domain preferring PyrSM recycled more effectively, by using Hrs-, Tsg101- and NPC1-independent routing that was insensitive to cholesterol loading. Similar chain length-dependent recycling was observed for unlabeled sphingomyelins (SMs). The findings 1) establish acyl chain length as an important determinant in the endocytic trafficking of SMs, 2) implicate ESCRT complex proteins and NPC1 in the endocytic recycling of ordered domain lipids to the plasma membrane, and 3) introduce long-chain PyrSM as the first fluorescent lipid tracing this pathway.

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