Enzymic synthesis of lignin precursors. Purification and properties of 4-coumarate:CoA ligase from cambial sap of spruce (Picea abies L.).
4-Coumarate:CoA ligase was purified from cambial sap of spruce (Picea abies). A 1627-fold purification of the enzyme with a yield of 37% was achieved by a six-step procedure including dye-ligand chromatography. Isozymes of the ligase were not detected. The enzyme has an Mr of about 63 000 and is a single polypeptide chain. Ferulic, 4-coumaric and caffeic acids are efficient substrates for the ligase. In contrast to some ligases from angiosperms, the ligase from spruce (gymnosperm) does not activate sinapic acid. The substrate specificity of the ligase is consistent with the lignin composition of spruce.
D003066:Coenzyme A Ligases / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008031:Lignin / Q000096:biosynthesis*; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity; D014197:Trees
D008031:Lignin; D003066:Coenzyme A Ligases; C019943:4-coumarate-CoA ligase