• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利：CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法，用中文像聊天一样搜索，搜遍4000万医学文献。AI智能推荐，让科研检索更轻松。

立即免费搜索

文件翻译

保留排版，准确专业，支持PDF/Word/PPT等文件格式，支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述，25分钟生成高质量综述，智能提取关键信息，辅助科研写作。

立即免费体验

Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity of Cr(III)ATP in the 3-phosphoglycerate kinase reaction. Structure of the metal nucleotide substrates.

作者信息

Jaffe E K, Nick J, Cohn M

出版信息

J Biol Chem. 1982 Jul 10;257(13):7650-6.

PMID:7045111
Abstract
摘要

相似文献

1
Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity of Cr(III)ATP in the 3-phosphoglycerate kinase reaction. Structure of the metal nucleotide substrates.ADP和ATP的硫代磷酸酯类似物的反应性及金属依赖性立体特异性，以及Cr(III)ATP在3-磷酸甘油酸激酶反应中的反应性。金属核苷酸底物的结构。
J Biol Chem. 1982 Jul 10;257(13):7650-6.
2
Diastereomers of the nucleoside phosphorothioates as probes of the structure of the metal nucleotide substrates and of the nucleotide binding site of yeast hexokinase.核苷硫代磷酸酯的非对映异构体作为金属核苷酸底物结构和酵母己糖激酶核苷酸结合位点的探针。
J Biol Chem. 1979 Nov 10;254(21):10839-45.
3
Interaction of ATP analogs with yeast 3-phosphoglycerate kinase. Affinity labeling of the hinge region.ATP类似物与酵母3-磷酸甘油酸激酶的相互作用。铰链区的亲和标记
Eur J Biochem. 1993 Mar 15;212(3):719-26. doi: 10.1111/j.1432-1033.1993.tb17710.x.
4
Shift of the equilibrium constant of the 3-P-glycerate kinase reaction towards 1,3-bis-P-glycerate with adenosine 5'-O-(2-thiotriphosphate) (ATP beta S) as substrate.以腺苷5'-O-(2-硫代三磷酸)(ATPβS)为底物时，3-磷酸甘油酸激酶反应的平衡常数向1,3-二磷酸甘油酸方向移动。
J Biol Chem. 1980 Apr 25;255(8):3240-1.
5
The possibility that the substrates of phosphoglycerate kinase may specifically regulate the direction of its reversible reaction [proceedings].
Biochem Soc Trans. 1977;5(3):770-1. doi: 10.1042/bst0050770.
6
Structure of the metal.nucleotide complex in the yeast phenylalanyl transfer ribonucleic acid synthetase reaction as determined with diastereomeric phosphorothioate analogs of ATP.利用ATP的非对映体硫代磷酸酯类似物确定的酵母苯丙氨酰转移核糖核酸合成酶反应中金属-核苷酸复合物的结构。
J Biol Chem. 1980 Dec 10;255(23):11301-7.
7
Structure of the metal-nucleotide complex in the acetate kinase reaction. A study with gamma-32P-labeled phosphorothioate analogs of ATP.
J Biol Chem. 1981 Jul 25;256(14):7322-8.
8
Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ATP in the arginine kinase reaction. Structure of the metal-nucleoside triphosphate substrate.精氨酸激酶反应中ATP硫代磷酸酯类似物的反应活性及金属依赖性立体特异性。金属核苷三磷酸底物的结构。
J Biol Chem. 1982 Jul 10;257(13):7646-9.
9
Substrate activity of Rh(III)ATP with phosphoglycerate kinase and the role of the metal ion in catalysis.铑（III）三磷酸腺苷与磷酸甘油酸激酶的底物活性以及金属离子在催化中的作用。
Arch Biochem Biophys. 1994 Jun;311(2):503-8. doi: 10.1006/abbi.1994.1268.
10
Structure of metal x nucleotide complex in the creatine kinase reaction. A study with diastereomeric phosphorothioate analogs of adenosine di- and triphosphate.肌酸激酶反应中金属x核苷酸复合物的结构。对腺苷二磷酸和三磷酸的非对映体硫代磷酸酯类似物的研究。
J Biol Chem. 1980 Sep 10;255(17):8229-33.

引用本文的文献

1
Antagonistic binding of substrates to 3-phosphoglycerate kinase monitored by the fluorescent analogue 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate.通过荧光类似物2'(3')-O-(2,4,6-三硝基苯基)腺苷5'-三磷酸监测底物与3-磷酸甘油酸激酶的拮抗结合。
Biochem J. 1994 Aug 1;301 ( Pt 3)(Pt 3):885-91. doi: 10.1042/bj3010885.
2
Stereoselectivity of ectonucleotidases on vascular endothelial cells.血管内皮细胞上外核苷酸酶的立体选择性
Biochem J. 1983 Sep 15;214(3):975-81. doi: 10.1042/bj2140975.
3
Characterization of the structure and properties of the His 62-->Ala and Arg 38-->Ala mutants of yeast phosphoglycerate kinase: an investigation of the catalytic and activatory sites by site-directed mutagenesis and NMR.
酵母磷酸甘油酸激酶His 62→Ala和Arg 38→Ala突变体的结构与性质表征：通过定点诱变和核磁共振对催化位点与激活位点的研究
Protein Sci. 1992 Jun;1(6):752-60. doi: 10.1002/pro.5560010607.