Discrimination between the regioisomeric 1,2- and 1,3-diacylglycerophosphocholines by phospholipases

Mansfeld, Johanna; Brandt, Wolfgang; Haftendorn, Regine; Schöps, Regina; Ulbrich‐Hofmann, Renate

doi:10.1016/j.chemphyslip.2010.12.009

Cited by 6 publications

(3 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Another mode as to how the substrate structure influences the catalytic efficiency is reflected by the cooperativity of substrate binding as expressed in the Hill coefficients ( Table 2). This cooperative behavior might be caused by regulatory substrate binding sites, as has been discussed for several monomeric PLA 2 s [56,57] or the formation of enzyme oligomers as described for many fungal phospholipases [40,44].…”

Section: Pla 1 Enzymes From a Ostoyae Are New Representatives Of Thementioning

confidence: 86%

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Dippe

Müller

Sinz

et al. 2012

J Americ Oil Chem Soc

View full text Add to dashboard Cite

Four enzymes with phospholipase A 1 (PLA 1 ) activity were purified from the fruiting bodies of the basidiomycete Armillaria ostoyae. The enzymes (PLA 1 -1, -2, -3 and -4) showed similar isoelectric points (4.3, 3.9, 4.0 and 4.0) and apparent molecular masses in the range of 35-47 kDa. Mass spectrometric analyses of proteolytic fragments revealed sequences homologous to a/b-hydrolase fold enzymes. The enzymes share one conserved region with fungal phospholipases B and the active site sequence with bacterial esterases and PLA 1 s. PLA 1 -1 cleaves phospholipids and lysophospholipids with an optimum activity at pH 5.3. In contrast, PLA 1 -2, -3 and -4 are characterized by broad pH optima in the slightly acidic to neutral range and are additionally capable of hydrolyzing mono-and diglycerides as well as fatty acid methyl esters. All enzymes favor glycerol-based lipids with a single medium-sized fatty acid moiety in the sn-1 position but show reduced activity towards the corresponding 1,2-diacyl derivatives with bulky long-chain or inflexible Data from mass-spectrometric peptide sequencing are available in the PRIDE database (http://www.ebi.ac.uk/pride/) under the accession numbers 17662-17665.Electronic supplementary material The online version of this article (

show abstract

Section: Pla 1 Enzymes From a Ostoyae Are New Representatives Of Thementioning

confidence: 86%

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Dippe

Müller

Sinz

et al. 2012

J Americ Oil Chem Soc

View full text Add to dashboard Cite

show abstract

“…For example, phospholipases 1 and 2 (PLA1 and PLA2) hydrolyze 1,2-diacyl-sn-glycero-3-phospholipids at either the sn-1 position (PLA1) or at the sn-2 position (PLA2). The related congener phospholipase C (PLC) hydrolyzes the same 1,2-diacyl-sn-glycero-3-phospholipids glycerophosphate bond, while phospholipase D (PLD) cleaves the terminal phosphodiester bond of the phospholipids, yielding phosphatidic acid [15]. Lipases, such as PLA1, PLA2, PLC and PLD outlined above, evolved to process natural amphiphiles, but they can also process their synthetic congeners; therefore, they were also considered in our study.…”

Section: Esterase and Lipase Activity Overview And Selection Of Repre...mentioning

confidence: 99%

“…Another survey of the literature available revealed two main methods that assess PLA2 activity based on quantitation of acid liberated during hydrolysis of phospholipids. Method 1 is essentially a pH stat method that employs an autotitrator [15,[48][49][50][51], while Method 2 involves bromothymol blue as a pH indicator [52,53]. We have selected bromothymol blue (BTB) as the indicator dye due to the fact that its color changes at around physiological pH (pH 6.0-7.6) [53,54].…”

Section: Pla2-specific Hydrolysis Of Phospholipidsmentioning

confidence: 99%

Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity

Lam

Ilies

2022

IJMS

View full text Add to dashboard Cite

Esterases and lipases can process amphiphilic esters used as drugs and prodrugs and impact their pharmacokinetics and biodistribution. These hydrolases can also process ester components of drug delivery systems (DDSs), thus triggering DDSs destabilization with premature cargo release. In this study we tested and optimized assays that allowed us to quantify and compare individual esterase contributions to the degradation of substrates of increased lipophilicity and to establish limitations in terms of substrates that can be processed by a specific esterase/lipase. We have studied the impact of carbonic anhydrase; phospholipases A1, A2, C and D; lipoprotein lipase; and standard lipase on the hydrolysis of 4-nitrophenyl acetate, 4-nitrophenyl palmitate, DGGR and POPC liposomes, drawing structure–property relationships. We found that the enzymatic activity of these proteins was highly dependent on the lipophilicity of the substrate used to assess them, as expected. The activity observed for classical esterases was diminished when lipophilicity of the substrate increased, while activity observed for lipases generally increased, following the interfacial activation model, and was highly dependent on the type of lipase and its structure. The assays developed allowed us to determine the most sensitive methods for quantifying enzymatic activity against substrates of particular types and lipophilicity.

show abstract

Synthesis of PhospholipidRibavirin Conjugates

Oleynikova

Кулак

Bolibrukh

et al. 2013

Helvetica Chimica Acta

View full text Add to dashboard Cite

New conjugates of antiviral nucleoside Ribavirin (=1‐(β‐D‐ribofuranosyl)‐1H‐1,2,4‐triazole‐3‐carboxamide; 1) with 1,2‐ and 1,3‐diacyl glycerophosphates have been synthesized by the phosphoramidite method. A combination of 2′,3′‐phenylboronate protecting group for the sugar moiety of the ribonucleoside 1 and 2‐cyanoethyl protection for the phosphate fragment ensured the preparation of the desired compounds with reasonable yields via a small number of synthetic steps.

show abstract

Discrimination between the regioisomeric 1,2- and 1,3-diacylglycerophosphocholines by phospholipases

Cited by 6 publications

References 51 publications

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity

Synthesis of PhospholipidRibavirin Conjugates

Contact Info

Product

Resources

About

Discrimination between the regioisomeric 1,2- and 1,3-diacylglycerophosphocholines by phospholipases

Cited by 6 publications

References 51 publications

Phospholipases A1 from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Phospholipases A1 from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity

Synthesis of PhospholipidRibavirin Conjugates

Contact Info

Product

Resources

About

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes