PURIFICATION AND PROPERTIES OF AMP-DEAMINASE FROM HUMAN UTERINE SMOOTH-MUSCLE - REGULATION BY ADENYLATE ENERGY-CHARGE AND ACTIVATED FATTY-ACIDS

被引：7

作者：

NOWAK, G ^{[1
]}

NAGELSTARCZYNOWSKA, G ^{[1
]}

KALETHA, K ^{[1
]}

机构：

[1] MED ACAD GDANSK,DEPT BIOCHEM,UL DEBINKI 1,PL-80211 GDANSK,POLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1991年 / 1078卷 / 02期

关键词：

ENZYME CHARACTERIZATION; AMP-DEAMINASE; ENZYME ACTIVITY REGULATION; (HUMAN UTERINE SMOOTH MUSCLE);

D O I：

10.1016/0167-4838(91)90573-I

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：

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.

引用

页码：303 / 304

页数：2

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