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4-coumarate:CoA ligase

4-coumaroyl-CoA (4CL) ligase belongs to the family of ligase and is an enzyme that catalyze the reaction below： ATP+4-coumarate+CoA AMP+ diphosphate+4-coumaroyl-CoA. Ligase in the enzymology, is is an enzyme that catalyze the joining of two large molecule by forming new chemical bond. In the process of catalysis, there is always hydrolysis of small molecule group accompanying. 4CL ligase catalyzes the formation of carbon sulfur bond between two reactants. 4CL is one of the key enzyme regulating the synthesis of monolignols in the lignin pathway. Lignin is an unique and complex phenylpropanoid polymer which plays key role in plant development and response to the environment. Lignin is typically polymerized from 3 phenylpropanoid mononers , p-coumaryl (H), coniferyl (G) and sinapyl (S). The relative amounts of these 3 monomers found in lignin show plant specificity and 4CL is one of the enzyme participating the formation these 3 monomers in the regulatory network of the monolignol pathway and has significant effect on the S/G ratio which is substantial to the lignin formation situation in the plant. There is report showing that the 4CL gene knock-down will result in the lignin reduction. 4CL is found having significant importance on regulation of the phenylpropanoid pathway by regulating the synthesis rates of different hydroxycinnamoyl CoA thioesters. In other words, the activity of 4CL determines the overall carbon flow of the phenylpropanoid pathway. For this reason, 4CL has been focused on the genetic engineering regulation about the plants products quality improvement.