Literature DB >> 4772281

Inhibition of 3-phosphoglycerate dehydrogenase from Pisum sativum by purine nucleotides.

J C Slaughter.   

Abstract

The inhibition of 3-phosphoglycerate dehydrogenase from etiolated pea epicotyls by purine nucleoside di- and tri-phosphates is linear, competitive with regard to NADH, and the nucleotides are mutually exclusive in their binding. Free ATP and ADP are more effective inhibitors than are the respective magnesium complexes.

Entities:  

Mesh：

Substances：

Year:  1973        PMID： 4772281      PMCID： PMC1165863          DOI： 10.1042/bj1350563

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  3 in total

1.  The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas.

Authors:  J C Slaughter; D D Davies
Journal:  Biochem J       Date:  1968-10       Impact factor: 3.857

2.  Studies on factors influencing enzyme responses to adenylate energy charge.

Authors:  D L Purich; H J Fromm
Journal:  J Biol Chem       Date:  1972-01-10       Impact factor: 5.157

3.  Inhibition of 3-phosphoglycerate dehydrogenase by l-serine.

Authors:  J C Slaughter; D D Davies
Journal:  Biochem J       Date:  1968-10       Impact factor: 3.857
  3 in total
  1 in total

1.  Effect of nucleoside di-and triphosphates and MgCl2 on the activity of 5'-nucleotidase from bull seminal plasma.

Authors:  C Fini; A Minelli; A Floridi; P L Ipata
Journal:  Experientia       Date:  1975-04-15
  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.