@article{lueking_sn-glycerol-3-phosphate_1975,
	title = {sn-{Glycerol}-3-phosphate acyltransferase activity in particulate preparations from anaerobic, light-grown cells of {Rhodopseudomonas} spheroides. {Involvement} of acyl thiolester derivatives of acyl carrier protein in the synthesis of complex lipids},
	volume = {250},
	issn = {0021-9258},
	abstract = {Crude particulate preparations obtained from anaerobic, light-grown cells of Rhodopseudomonas spheroides have been shown to possess a significant level of sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.15) activity. In contrast to the enzyme from Escherichia coli, the R. spheroides glycerophosphate acyltransferase has a high specificity for acyl thiolester derivatives of acyl carrier protein (ACP) as acyl donors for the reaction. Only limited , nonlinear glycerophosphate incorporation into lipid occurs when acyl coenzyme A (CoA) derivatives are employed as acyl substrate. With oleyl-ACP as substrate, maximal enzyme activity was observed at 40 degrees, over a broad pH range (6.0 to 8.5) and did not require a divalent metal cation. The presence of dithiothreitol stimulated enzyme-activity 15 to 20\%. When oleyl-ACP or palmityl-ACP was employed as sole acyl group donor, the major products recoverable from the reaction mixtures were lysophosphatidic acid, phosphatidic acid, and monoglyceride. Althouh oleyl-ACP and palmityl-ACP gave comparable maximal velocities in the initial acylation of glycerophosphate, the formation of phosphatidic acid occurred preferentially with the unsaturated acyl-ACP derivative.},
	language = {eng},
	number = {21},
	journal = {The Journal of Biological Chemistry},
	author = {Lueking, D. R. and Goldfine, H.},
	month = nov,
	year = {1975},
	pmid = {387},
	keywords = {Acyltransferases, Anaerobiosis, Bacteriochlorophylls, Glycerophosphates, Hydrogen-Ion Concentration, Kinetics, Light, Rhodobacter sphaeroides, Temperature},
	pages = {8530--8535}
}

{"_id":"hCYRLdHRSqpANm9zT","bibbaseid":"lueking-goldfine-snglycerol3phosphateacyltransferaseactivityinparticulatepreparationsfromanaerobiclightgrowncellsofrhodopseudomonasspheroidesinvolvementofacylthiolesterderivativesofacylcarrierproteininthesynthesisofcomplexlipids-1975","authorIDs":[],"author_short":["Lueking, D. R.","Goldfine, H."],"bibdata":{"bibtype":"article","type":"article","title":"sn-Glycerol-3-phosphate acyltransferase activity in particulate preparations from anaerobic, light-grown cells of Rhodopseudomonas spheroides. Involvement of acyl thiolester derivatives of acyl carrier protein in the synthesis of complex lipids","volume":"250","issn":"0021-9258","abstract":"Crude particulate preparations obtained from anaerobic, light-grown cells of Rhodopseudomonas spheroides have been shown to possess a significant level of sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.15) activity. In contrast to the enzyme from Escherichia coli, the R. spheroides glycerophosphate acyltransferase has a high specificity for acyl thiolester derivatives of acyl carrier protein (ACP) as acyl donors for the reaction. Only limited , nonlinear glycerophosphate incorporation into lipid occurs when acyl coenzyme A (CoA) derivatives are employed as acyl substrate. With oleyl-ACP as substrate, maximal enzyme activity was observed at 40 degrees, over a broad pH range (6.0 to 8.5) and did not require a divalent metal cation. The presence of dithiothreitol stimulated enzyme-activity 15 to 20%. When oleyl-ACP or palmityl-ACP was employed as sole acyl group donor, the major products recoverable from the reaction mixtures were lysophosphatidic acid, phosphatidic acid, and monoglyceride. Althouh oleyl-ACP and palmityl-ACP gave comparable maximal velocities in the initial acylation of glycerophosphate, the formation of phosphatidic acid occurred preferentially with the unsaturated acyl-ACP derivative.","language":"eng","number":"21","journal":"The Journal of Biological Chemistry","author":[{"propositions":[],"lastnames":["Lueking"],"firstnames":["D.","R."],"suffixes":[]},{"propositions":[],"lastnames":["Goldfine"],"firstnames":["H."],"suffixes":[]}],"month":"November","year":"1975","pmid":"387","keywords":"Acyltransferases, Anaerobiosis, Bacteriochlorophylls, Glycerophosphates, Hydrogen-Ion Concentration, Kinetics, Light, Rhodobacter sphaeroides, Temperature","pages":"8530–8535","bibtex":"@article{lueking_sn-glycerol-3-phosphate_1975,\n\ttitle = {sn-{Glycerol}-3-phosphate acyltransferase activity in particulate preparations from anaerobic, light-grown cells of {Rhodopseudomonas} spheroides. {Involvement} of acyl thiolester derivatives of acyl carrier protein in the synthesis of complex lipids},\n\tvolume = {250},\n\tissn = {0021-9258},\n\tabstract = {Crude particulate preparations obtained from anaerobic, light-grown cells of Rhodopseudomonas spheroides have been shown to possess a significant level of sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.15) activity. In contrast to the enzyme from Escherichia coli, the R. spheroides glycerophosphate acyltransferase has a high specificity for acyl thiolester derivatives of acyl carrier protein (ACP) as acyl donors for the reaction. Only limited , nonlinear glycerophosphate incorporation into lipid occurs when acyl coenzyme A (CoA) derivatives are employed as acyl substrate. With oleyl-ACP as substrate, maximal enzyme activity was observed at 40 degrees, over a broad pH range (6.0 to 8.5) and did not require a divalent metal cation. The presence of dithiothreitol stimulated enzyme-activity 15 to 20\\%. When oleyl-ACP or palmityl-ACP was employed as sole acyl group donor, the major products recoverable from the reaction mixtures were lysophosphatidic acid, phosphatidic acid, and monoglyceride. Althouh oleyl-ACP and palmityl-ACP gave comparable maximal velocities in the initial acylation of glycerophosphate, the formation of phosphatidic acid occurred preferentially with the unsaturated acyl-ACP derivative.},\n\tlanguage = {eng},\n\tnumber = {21},\n\tjournal = {The Journal of Biological Chemistry},\n\tauthor = {Lueking, D. R. and Goldfine, H.},\n\tmonth = nov,\n\tyear = {1975},\n\tpmid = {387},\n\tkeywords = {Acyltransferases, Anaerobiosis, Bacteriochlorophylls, Glycerophosphates, Hydrogen-Ion Concentration, Kinetics, Light, Rhodobacter sphaeroides, Temperature},\n\tpages = {8530--8535}\n}\n\n","author_short":["Lueking, D. R.","Goldfine, H."],"key":"lueking_sn-glycerol-3-phosphate_1975","id":"lueking_sn-glycerol-3-phosphate_1975","bibbaseid":"lueking-goldfine-snglycerol3phosphateacyltransferaseactivityinparticulatepreparationsfromanaerobiclightgrowncellsofrhodopseudomonasspheroidesinvolvementofacylthiolesterderivativesofacylcarrierproteininthesynthesisofcomplexlipids-1975","role":"author","urls":{},"keyword":["Acyltransferases","Anaerobiosis","Bacteriochlorophylls","Glycerophosphates","Hydrogen-Ion Concentration","Kinetics","Light","Rhodobacter sphaeroides","Temperature"],"downloads":0,"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/w_cools","creationDate":"2020-06-07T16:33:24.865Z","downloads":0,"keywords":["acyltransferases","anaerobiosis","bacteriochlorophylls","glycerophosphates","hydrogen-ion concentration","kinetics","light","rhodobacter sphaeroides","temperature"],"search_terms":["glycerol","phosphate","acyltransferase","activity","particulate","preparations","anaerobic","light","grown","cells","rhodopseudomonas","spheroides","involvement","acyl","thiolester","derivatives","acyl","carrier","protein","synthesis","complex","lipids","lueking","goldfine"],"title":"sn-Glycerol-3-phosphate acyltransferase activity in particulate preparations from anaerobic, light-grown cells of Rhodopseudomonas spheroides. Involvement of acyl thiolester derivatives of acyl carrier protein in the synthesis of complex lipids","year":1975,"dataSources":["DPzNnv8mwEoHbb7Cq"]}