Phosphatidylethanolamine methyltransferase and phospholipid methyltransferase activities from Saccharomyces cerevisiae. Enzymological and kinetic properties

Gaynor, P.M.; Carman, G.M.; Biochim. Biophys. Acta 1045, 156-163 (1990)

Data extracted from this reference:

Cloned(Commentary)

Commentary	Organism
enzyme is encoded by PEM2/OPI3 gene, cloned by complementation	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Commentary	Organism	Structure
HgCl2	-	Saccharomyces cerevisiae
Octyl glucoside	-	Saccharomyces cerevisiae
p-Chloromercuriphenylsulfonic acid	-	Saccharomyces cerevisiae
S-adenosyl-L-homocysteine	-	Saccharomyces cerevisiae
Sodium cholate	-	Saccharomyces cerevisiae
Triton X-100	-	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Commentary	Organism	Structure
0.054	-	phosphatidyl-N-monomethylethanolamine	-	Saccharomyces cerevisiae
0.059	-	phosphatidyl-N-dimethylethanolamine	-	Saccharomyces cerevisiae
0.18	-	phosphatidyl-N-dimethylethanolamine	-	Saccharomyces cerevisiae
0.38	-	phosphatidyl-N-monomethylethanolamine	-	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Commentary	Organism	Structure
Ca2+	leads to a stimulation of activity	Saccharomyces cerevisiae
Mg2+	leads to a stimulation of activity	Saccharomyces cerevisiae

Organism

Organism	Primary Accession No. (UniProt)	Commentary	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Commentary Substrates	Literature (Substrates)	Organism	Products	Commentary (Products)	Literature (Products)	Organism (Products)	Reversibility
S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine	-	485166	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + phosphatidylcholine	-	-	-	?
S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine	-	485166	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine	-	-	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Commentary	Organism
40	-	-	Saccharomyces cerevisiae

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Commentary	Organism
30	-	unstable above	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Commentary	Organism
7.5	-	-	Saccharomyces cerevisiae

pH Range

pH Minimum	pH Maximum	Commentary	Organism
6.5	9.5	-	Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Commentary	Organism	Structure
0.054	-	S-adenosyl-L-homocysteine	phosphatidyl-N-dimethylethanolamine as substrate, competitive inhibition	Saccharomyces cerevisiae
0.057	-	S-adenosyl-L-homocysteine	phosphatidyl-N-monomethylethanolamine as substrate, competitive inhibition	Saccharomyces cerevisiae
0.12	-	S-adenosyl-L-homocysteine	phosphatidyl-N-dimethylethanolamine as substrate, noncompetitive inhibition	Saccharomyces cerevisiae
0.32	-	S-adenosyl-L-homocysteine	phosphatidyl-N-monomethylethanolamine as substrate, noncompetitive inhibition	Saccharomyces cerevisiae

Cloned(Commentary) (protein specific)

Commentary	Organism
enzyme is encoded by PEM2/OPI3 gene, cloned by complementation	Saccharomyces cerevisiae

Inhibitors (protein specific)

Inhibitors	Commentary	Organism	Structure
HgCl2	-	Saccharomyces cerevisiae
Octyl glucoside	-	Saccharomyces cerevisiae
p-Chloromercuriphenylsulfonic acid	-	Saccharomyces cerevisiae
S-adenosyl-L-homocysteine	-	Saccharomyces cerevisiae
Sodium cholate	-	Saccharomyces cerevisiae
Triton X-100	-	Saccharomyces cerevisiae

Ki Value [mM] (protein specific)

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Commentary	Organism	Structure
0.054	-	S-adenosyl-L-homocysteine	phosphatidyl-N-dimethylethanolamine as substrate, competitive inhibition	Saccharomyces cerevisiae
0.057	-	S-adenosyl-L-homocysteine	phosphatidyl-N-monomethylethanolamine as substrate, competitive inhibition	Saccharomyces cerevisiae
0.12	-	S-adenosyl-L-homocysteine	phosphatidyl-N-dimethylethanolamine as substrate, noncompetitive inhibition	Saccharomyces cerevisiae
0.32	-	S-adenosyl-L-homocysteine	phosphatidyl-N-monomethylethanolamine as substrate, noncompetitive inhibition	Saccharomyces cerevisiae

KM Value [mM] (protein specific)

KM Value [mM]	KM Value Maximum [mM]	Substrate	Commentary	Organism	Structure
0.054	-	phosphatidyl-N-monomethylethanolamine	-	Saccharomyces cerevisiae
0.059	-	phosphatidyl-N-dimethylethanolamine	-	Saccharomyces cerevisiae
0.18	-	phosphatidyl-N-dimethylethanolamine	-	Saccharomyces cerevisiae
0.38	-	phosphatidyl-N-monomethylethanolamine	-	Saccharomyces cerevisiae

Metals/Ions (protein specific)

Metals/Ions	Commentary	Organism	Structure
Ca2+	leads to a stimulation of activity	Saccharomyces cerevisiae
Mg2+	leads to a stimulation of activity	Saccharomyces cerevisiae

Substrates and Products (Substrate) (protein specific)

Substrates	Commentary Substrates	Literature (Substrates)	Organism	Products	Commentary (Products)	Literature (Products)	Organism (Products)	Reversibility
S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine	-	485166	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + phosphatidylcholine	-	-	-	?
S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine	-	485166	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine	-	-	-	?

Temperature Optimum [°C] (protein specific)

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Commentary	Organism
40	-	-	Saccharomyces cerevisiae

Temperature Stability [°C] (protein specific)

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Commentary	Organism
30	-	unstable above	Saccharomyces cerevisiae

pH Optimum (protein specific)

pH Optimum Minimum	pH Optimum Maximum	Commentary	Organism
7.5	-	-	Saccharomyces cerevisiae

pH Range (protein specific)

pH Minimum	pH Maximum	Commentary	Organism
6.5	9.5	-	Saccharomyces cerevisiae

See also following references to EC number 2.1.1.71 (sorted by year of publication):

No.	1st author	Pub Med	title	organims	journal	volume	pages	year	Activating Compound	Application	Cloned(Commentary)	Crystallization (Commentary)	Engineering	General Stability	Inhibitors	KM Value [mM]	Localization	Metals/Ions	Molecular Weight [Da]	Natural Substrates/ Products (Substrates)	Organic Solvent Stability	Organism	Oxidation Stability	Posttranslational Modification	Purification (Commentary)	Reaction	Renatured (Commentary)	Source Tissue	Specific Activity [micromol/min/mg]	Storage Stability	Substrates and Products (Substrate)	Subunits	Temperature Optimum [°C]	Temperature Range [°C]	Temperature Stability [°C]	Turnover Number [1/s]	pH Optimum	pH Range	pH Stability	Cofactor	Ki Value [mM]	pI Value	IC50 Value	Activating Compound (protein specific)	Application (protein specific)	Cloned(Commentary) (protein specific)	Cofactor (protein specific)	Crystallization (Commentary) (protein specific)	Engineering (protein specific)	General Stability (protein specific)	IC50 Value (protein specific)	Inhibitors (protein specific)	Ki Value [mM] (protein specific)	KM Value [mM] (protein specific)	Localization (protein specific)	Metals/Ions (protein specific)	Molecular Weight [Da] (protein specific)	Natural Substrates/ Products (Substrates) (protein specific)	Organic Solvent Stability (protein specific)	Oxidation Stability (protein specific)	Posttranslational Modification (protein specific)	Purification (Commentary) (protein specific)	Renatured (Commentary) (protein specific)	Source Tissue (protein specific)	Specific Activity [micromol/min/mg] (protein specific)	Storage Stability (protein specific)	Substrates and Products (Substrate) (protein specific)	Subunits (protein specific)	Temperature Optimum [°C] (protein specific)	Temperature Range [°C] (protein specific)	Temperature Stability [°C] (protein specific)	Turnover Number [1/s] (protein specific)	pH Optimum (protein specific)	pH Range (protein specific)	pH Stability (protein specific)	pI Value (protein specific)	Expression	General Information	General Information (protein specific)	Expression (protein specific)	KCat/KM [mM/s]	KCat/KM [mM/s] (protein specific)
704482	Keogh		Functional characterization of ...	Arabidopsis thaliana, Glycine max	J. Biol. Chem.	284	15439-15447	2009	-	-	2	-	-	-	-	-	2	-	-	-	-	2	-	-	-	-	-	-	-	-	6	-	-	-	-	-	-	-	-	-	-	-	-	-	-	2	-	-	-	-	-	-	-	-	2	-	-	-	-	-	-	-	-	-	-	-	6	-	-	-	-	-	-	-	-	-	-	1	1	-	-	-
485190	Guan		Activity of phosphatidylethano ...	Homo sapiens	Neurochem. Int.	34	41-47	1999	-	-	-	-	-	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-
485557	Kanipes		The phospholipid methyltransfe ...	Bos taurus, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Schizosaccharomyces pombe	Biochim. Biophys. Acta	1348	134-141	1997	-	-	4	-	-	-	-	-	2	-	1	-	-	5	-	-	-	-	-	2	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	4	-	-	-	-	-	-	-	-	2	-	1	-	-	-	-	-	-	2	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-
485559	Iliskovic		Adriamycin depresses in vivo a ...	Rattus norvegicus	Mol. Cell. Biochem.	176	235-240	1997	-	1	-	-	-	-	1	-	-	-	-	-	-	1	-	-	-	-	-	1	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	-	1	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-
485193	Roque		Phosphatidylethanolamine N-met ...	Bos taurus, Rattus norvegicus	Exp. Eye Res.	60	631-643	1995	-	-	-	-	-	-	-	2	5	1	-	-	-	2	-	-	1	-	-	3	-	-	4	-	-	-	-	-	3	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	2	5	1	-	-	-	-	-	1	-	3	-	-	4	-	-	-	-	-	3	1	-	-	-	-	-	-	-	-
485166	Gaynor		Phosphatidylethanolamine methy ...	Saccharomyces cerevisiae	Biochim. Biophys. Acta	1045	156-163	1990	-	-	1	-	-	-	6	4	-	2	-	-	-	2	-	-	-	-	-	-	-	-	2	-	1	-	1	-	1	1	-	-	4	-	-	-	-	1	-	-	-	-	-	6	4	4	-	2	-	-	-	-	-	-	-	-	-	-	2	-	1	-	1	-	1	1	-	-	-	-	-	-	-	-
485561	Tanaka		Purification and properties of ...	Mus musculus	Jpn. J. Med. Sci. Biol.	43	59-73	1990	-	-	-	-	-	-	-	-	-	-	-	-	-	1	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-
485562	Pilarska		Properties and topology of enz ...	Oryctolagus cuniculus	Int. J. Biochem.	19	705-711	1987	-	-	-	-	-	-	-	-	1	-	-	-	-	1	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-
485560	Sastry		Evidence for two methyltransfe ...	Bos taurus, Homo sapiens, Neurospora crassa, Rattus norvegicus	Arch. Biochem. Biophys.	211	762-773	1981	-	-	-	-	-	-	-	2	6	-	-	-	-	4	-	-	-	-	-	8	-	-	4	-	-	-	-	-	2	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	2	6	-	-	-	-	-	-	-	-	8	-	-	4	-	-	-	-	-	2	1	-	-	-	-	-	-	-	-
485554	Schneider		Conversion of phosphatidyletha ...	Rattus norvegicus	J. Biol. Chem.	254	3886-3891	1979	-	-	-	-	-	-	3	3	2	-	-	-	-	1	-	-	1	-	-	2	1	2	4	-	-	-	-	-	1	1	-	-	2	-	-	-	-	-	-	-	-	-	-	3	2	3	2	-	-	-	-	-	-	1	-	2	1	2	4	-	-	-	-	-	1	1	-	-	-	-	-	-	-	-
485555	Hirata		Identification and properties ...	Bos taurus, Neurospora crassa, Rattus norvegicus	Proc. Natl. Acad. Sci. USA	75	1718-1721	1978	-	-	-	-	-	-	-	1	4	-	-	-	-	3	-	-	-	-	-	4	-	-	5	-	-	-	-	-	2	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	1	4	-	-	-	-	-	-	-	-	4	-	-	5	-	-	-	-	-	2	-	-	-	-	-	-	-	-	-