Nucleotidyl Cyclase Activity of Soluble Guanylyl Cyclase α1β1

被引：65

作者：

Beste, Kerstin Y. ^{[1
]}

Burhenne, Heike ^{[1
]}

Kaever, Volkhard ^{[1
]}

Stasch, Johannes-Peter ^{[2
]}

Seifert, Roland ^{[1
]}

机构：

[1] Hannover Med Sch, Inst Pharmacol, D-30625 Hannover, Germany

[2] Bayer HealthCare, Inst Cardiovasc Res, Wuppertal, Germany

来源：

BIOCHEMISTRY | 2012年 / 51卷 / 01期

关键词：

CYTIDINE; 3'; 5'-MONOPHOSPHATE CCMP; DEPENDENT PROTEIN-KINASES; ADENYLYL-CYCLASE; NITRIC-OXIDE; BOVINE LUNG; CYTIDYLATE CYCLASE; PYRIMIDINE NUCLEOTIDES; RAT-TISSUES; DIFFERENTIAL INHIBITION; SUBSTRATE-SPECIFICITY;

D O I：

10.1021/bi201259y

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Soluble guanylyl cyclase (sGC) regulates several important physiological processes by converting GTP into the second-messenger cGMP. sGC has several structural and functional properties in common with adenylyl cyclases (ACs). Recently, we reported that membranous ACs and sGC are potently inhibited by 2',3'-O-(2,4,6-trinitrophenyl)-substituted purine and pyrimidine nucleoside 5'-triphosphates. Using a highly sensitive high-performance liquid chromatography tandem mass spectrometry method, we report that highly purified recombinant sGC of rat possesses nucleotidyl cyclase activity. As opposed to GTP, ITP, XTP and ATP, the pyrimidine nucleotides UTP and CTP were found to be sGC substrates in the presence of Mn2+. When Mg2+ is used, sGC generates cGMP, cAMP, cIMP, and cXMP. In conclusion, soluble "guanylyl" cyclase possesses much broader substrate specificity than previously assumed. Our data have nucleotide-mediated signal transduction. important implications for cyclic

引用

页码：194 / 204

页数：11

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