人子宫平滑肌中AMP脱氨酶的纯化及性质。腺苷酸能荷和活化脂肪酸的调节作用。

Purification and properties of AMP-deaminase from human uterine smooth muscle. Regulation by adenylate energy charge and activated fatty acids.

作者信息

Nowak G, Nagel-Starczynowska G, Kaletha K

机构信息

Department of Biochemistry, Academic Medical School, Gdańsk, Poland.

出版信息

Biochim Biophys Acta. 1991 Jun 24;1078(2):303-4. doi: 10.1016/0167-4838(91)90573-i.

DOI:10.1016/0167-4838(91)90573-i

PMID:2065099

Abstract

At pH 7.0 and physiological concentrations of the main regulatory ligands (ATP, ADP, orthophosphate), human uterine muscle AMP-deaminase follows a hyperbolic type of saturation kinetics with S0.5 parameter value about 2 mM. The enzyme is regulated by adenylate energy charge (AEC) variations, being the most active at the AEC value 0.5-0.6 or 0.5-0.7, depending on the size of the total adenine nucleotide pool. Long-chain acyl-CoA strongly inhibit activity of the enzyme, influencing mainly the maximum velocity of the reaction.

摘要

在pH 7.0以及主要调节性配体（ATP、ADP、正磷酸盐）的生理浓度条件下，人子宫肌AMP脱氨酶呈现双曲线型饱和动力学，其S0.5参数值约为2 mM。该酶受腺苷酸能荷（AEC）变化的调节，根据总腺嘌呤核苷酸池的大小，在AEC值为0.5 - 0.6或0.5 - 0.7时活性最高。长链酰基辅酶A强烈抑制该酶的活性，主要影响反应的最大速度。