The substrate requirements of phospholipase D

被引：9

作者：

Bossi, L

D'Arrigo, P

Pedrocchi-Fantoni, G

Mele, A

Servi, S

Leiros, I

机构：

[1] Politecn Milan, Dipartimento Chim, CNR, Ctr Studio Sostanze Organ Nat, I-20131 Milan, Italy

[2] Univ Tromso, Dept Chem, Fac Sci, N-9037 Tromso, Norway

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2001年 / 11卷 / 4-6期

关键词：

substrate; phospholipase D; hydrolysis;

D O I：

10.1016/S1381-1177(00)00157-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The hydrolysis rates of different diphosphates, compared with the one observed with natural phosphatidylcholine, are used to identify the molecular basis for phospholipase D (PLD) catalysis. Experimental data strongly support the idea that PLD is a rather generic phosphodiesterase with very wide substrate specificity and a net preference for Lipophilic substrates. The presence of choline in the polar head is not required for activity although it improves hydrolysis efficiency. Choline esters are found to be substrates for PLD hydrolysis, but only with long chain fatty acids. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：433 / 438

页数：6

共 17 条

[1] CATION-PI INTERACTION BETWEEN THE TRIMETHYLAMMONIUM MOIETY AND THE AROMATIC RING WITH INDOLE-3-ACETIC-ACID CHOLINE ESTER, A MODEL-COMPOUND FOR MOLECULAR RECOGNITION BETWEEN ACETYLCHOLINE AND ITS ESTERASE - AN X-RAY STUDY [J].