NDLI: Phospholipases A$_{1}$ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β-Hydrolase Fold Enzymes

Content Provider	Springer Nature Link
Author	Dippe, Martin Müller, Mathias Q. Sinz, Andrea Ulbrich Hofmann, Renate
Copyright Year	2012
Abstract	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 α/β-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 saturated fatty acid moieties in the sn-2 position. The enzymes prefer zwitterionic phospholipid substrates and are unable to hydrolyze triglycerides. From the selectivity of these broad-spectrum α/β-hydrolase fold enzymes towards the different classes of their substrates a regiospecific steric hindrance and a head group recognition are concluded.
Starting Page	1435
Ending Page	1448
Page Count	14
File Format	PDF
ISSN	0003021X
Journal	Journal of the American Oil Chemists' Society
Volume Number	89
Issue Number	8
e-ISSN	15589331
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-03-18
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Armillaria ostoyae Fatty acid specificity α/β-Hydrolase fold enzyme Phospholipase A$_{1}$ Substrate selectivity Agriculture Food Science Biomaterials Biotechnology Industrial Chemistry/Chemical Engineering
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Chemical Engineering

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