Abstract
1. The presence of palmitoyl-CoA-l-glycerol 1-phosphate palmitoyltransferase (EC2.3.1.15) has been demonstrated in a particulate fraction of baker's yeast. 2. The enzyme has been characterized, and its activity studied as a function of pH and concentration of substrates. 3. Inhibition by thiol poisons and protection by acyl-CoA have been used to obtain information on the active site. 4. By various methods of supplying acyl radicals, the species ;palmitoyl-CoA' has been shown to be the true acyl donor to the transferase.
Keywords
ACYLTRANSFERASES
AMIDES
CATALYSIS
CHROMATOGRAPHY
COENZYME A
ENZYME INHIBITORS
ETHYLMALEIMIDE
EXPERIMENTAL LAB STUDY
GLYCEROPHOSPHATES
HYDROGEN-ION CONCENTRATION
LIGASES
OLEIC ACID
PALMITIC ACID
PHARMACOLOGY
PHOSPHOLIPID METABOLISM
PYRROLES
SACCHAROMYCES
MeSH Terms
Acyl Coenzyme A
Acyltransferases
Amides
Catalysis
Chromatography
Coenzyme A
Enzyme Inhibitors
Ethylmaleimide
Glycerophosphates
Hydrogen-Ion Concentration
Ligases
Lipid Metabolism
Oleic Acid
Oleic Acids
Palmitic Acid
Palmitoyl Coenzyme A
Pharmacology
Phosphatidic Acids
Phospholipids/metabolism
Pyrroles
Research
Saccharomyces
Chemicals
Acyl Coenzyme A
Amides
Enzyme Inhibitors
Glycerophosphates
Oleic Acids
Phosphatidic Acids
Phospholipids
Pyrroles
Palmitoyl Coenzyme A
Oleic Acid
Palmitic Acid
alpha-glycerophosphoric acid
Acyltransferases
Ligases
Ethylmaleimide
Coenzyme A
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
KUHN N J
LYNEN F
References (18)
18 references, click to expand
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