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木质素前体的酶促合成。云杉(欧洲云杉)形成层汁液中4-香豆酸:辅酶A连接酶的纯化及性质

Enzymic synthesis of lignin precursors. Purification and properties of 4-coumarate:CoA ligase from cambial sap of spruce (Picea abies L.).

作者信息

Lüderitz T, Schatz G, Grisebach H

出版信息

Eur J Biochem. 1982 Apr;123(3):583-6.

PMID:7075602
Abstract

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.

摘要

4-香豆酸:辅酶A连接酶是从云杉(欧洲云杉)形成层汁液中纯化得到的。通过包括染料配体色谱法在内的六步程序,该酶实现了1627倍的纯化,产率为37%。未检测到连接酶的同工酶。该酶的分子量约为63000,是一条单多肽链。阿魏酸、4-香豆酸和咖啡酸是该连接酶的有效底物。与一些被子植物的连接酶不同,云杉(裸子植物)的连接酶不激活芥子酸。该连接酶的底物特异性与云杉的木质素组成一致。

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