Fatty acid selectivity of a lipase purified from Vernonia galamensis seed

Ncube, Ignatious; Gitlesen, Thomas; Adlercreutz, Patrick; Read, John S.; Mattìasson, Bo

doi:10.1016/0005-2760(95)00067-m

Cited by 39 publications

(25 citation statements)

References 25 publications

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“…The beans were soaked in running water for 1 day and germinated in the dark on moist vermiculite at 30°C. All reagents were obtained from Sigma, except for glycerol tri [1][2][3][4][5][6][7][8][9][10][11][12][13][14] C]oleate that was from Amersham Biosciences. Antibodies raised against the ϳ60-kDa band (RcOBL1) from castor bean oil body membranes (15) were provided by Dr. Mustak A. Kaderbhai, at the Institute of Biological Sciences, University of Wales, Aberystwyth, UK.…”

Section: Methodsmentioning

confidence: 99%

“…However, studies using electron microscopy have indicated that oil bodies are in close proximity with other organelles (particularly glyoxysomes), and it has long been hypothesized that an association between them may be required to facilitate fatty acid release and transfer (5,6). Lipases have been purified to apparent homogeneity from the seeds of several plants such as maize (Zea maize) (7), castor (Ricinus communis) (8,9), and ironweed (Vernonia galamensis) (10). However, most surprisingly none of the genes that encode these enzymes have been cloned and characterized.…”

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confidence: 99%

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Cloning and Characterization of the Acid Lipase from Castor Beans

Eastmond

2004

Journal of Biological Chemistry

124

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Castor bean endosperm contains a well known acid lipase activity that is associated with the oil body membrane. In order to identify this enzyme, proteomic analysis was performed on purified oil bodies. A ϳ60-kDa protein was identified (RcOBL1), which shares homology with a lipase from the filamentous fungus Rhizomucor miehei. RcOBL1 contains features that are characteristic of an ␣/␤-hydrolase, such as a putative catalytic triad (SDH) and a conserved pentapeptide (GXSXG) surrounding the nucleophilic serine residue. RcOBL1 was expressed heterologously in Escherichia coli and shown to hydrolyze triolein at an acid pH (optima ϳ4.5). RcOBL1 can hydrolyze a range of triacylglycerols but is not active on phospholipids. The activity is sensitive to the serine reagent diethyl p-nitrophenyl phosphate, indicating that RcOBL1 is a serine esterase. Antibodies raised against RcOBL1 were used to show that the protein is restricted to the endosperm where it is associated with the surface of oil bodies. This is the first evidence for the molecular identity of an oil body-associated lipase from plants. Sequence comparisons reveal that families of OBL1-like proteins are present in many species, and it is likely that they play an important role in regulating lipolysis.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

Cloning and Characterization of the Acid Lipase from Castor Beans

Eastmond

2004

Journal of Biological Chemistry

124

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“…Lipases have been purified from the seeds of plants such as maize (Zea mays) [19], castor bean (Ricinus communis) [20,21], oilseed rape [22] and ironweed (Vernonia galamensis) [23]. More recently, several genes have been cloned that encode proteins with TAG lipase activity from castor bean, Arabidopsis and tomato (Solanum lycopersicum) [24][25][26].…”

Section: Purification and Cloning Of Candidate Lipasesmentioning

confidence: 99%

“…Where a single molecular class of TAG predominates in the seed it appears that selective pressure has yielded a lipase with the appropriate specificity to hydrolyse that TAG following germination [46]. Among the most extreme examples of this typoselectivity appear to be the lipases from ironweed and Cuphea procumbans, which have been reported to exhibit more than 20-fold selectivity for trivernolin and tricaprin, respectively [23,46]. Because PTL functions are remarkably conserved between animals, yeast and Arabidopsis, it is likely that PTLs are involved in TAG breakdown in other plant species, although this remains to be demonstrated.…”

Section: Substrate Specificitymentioning

confidence: 99%

Storage oil hydrolysis during early seedling growth

Quettier

Eastmond

2009

Plant Physiology and Biochemistry

137

105

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Storage oil breakdown plays an important role in the life cycle of many plants by providing the carbon skeletons that support seedling growth immediately following germination. This metabolic process is initiated by lipases (EC: 3.1.1.3), which catalyse the hydrolysis of triacylglycerols (TAGs) to release free fatty acids and glycerol. A number of lipases have been purified to near homogeneity from seed tissues and analysed for their in vitro activities.Furthermore, several genes encoding lipases have been cloned and characterized from plants.However, only recently has data been presented to establish the molecular identity of a lipase that has been shown to be required for TAG breakdown in seeds. In this review we briefly outline the processes of TAG synthesis and breakdown. We then discuss some of the biochemical literature on seed lipases and describe the cloning and characterization of a lipase called SUGAR-DEPENDENT1, which is required for TAG breakdown in Arabidopsis thaliana seeds. presented to establish the molecular identity of a lipase that has been shown to be required for TAG breakdown in seeds. In this review we briefly outline the processes of TAG synthesis and breakdown. We then discuss some of the biochemical literature on seed lipases and describe the cloning and characterization of a lipase called SUGAR-DEPENDENT1, which is required for TAG breakdown in Arabidopsis thaliana seeds.

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“…The precipitates obtained were dissolved in 0.1 M Tris-HCl buffer (pH 7.0). To prepare an acetone powder, the germinated seeds were ground in ice-cold acetone and then washed several times with the cold acetone (Ncube et al, 1995). Lipase (glycerol ester hydrolase, E.C.…”

Section: Water Uptakementioning

confidence: 99%