Literature DB >> 1707371

Chloroplast phosphoribulokinase associates with yeast phosphoriboisomerase in the presence of substrate.

C L Skrukrud1, L E Anderson.   

Abstract

Pea chloroplastic phosphoribulokinase and yeast phosphoriboisomerase partition independently of one another in a two-phase polyethyleneglycol, dextran system, but apparent interaction is seen when ribose-5-phosphate is added to the two-phase system. It appears that the pea leaf kinase recognizes yeast isomerase when it is carrying metabolite.

Entities:  

Mesh：

Substances：

Year:  1991        PMID： 1707371     DOI： 10.1016/0014-5793(91)80306-n

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  2 in total

1.  Purification and characterization of pea chloroplastic phosphoriboisomerase.

Authors:  C L Skrukrud; I M Gordon; S Dorwin; X H Yuan; G Johansson; L E Anderson
Journal:  Plant Physiol       Date:  1991-10       Impact factor: 8.340

2.  Microsequencing and cDNA cloning of the Calvin cycle/OPPP enzyme ribose-5-phosphate isomerase (EC 5.3.1.6) from spinach chloroplasts.

Authors:  W Martin; K Henze; J Kellerman; A Flechner; C Schnarrenberger
Journal:  Plant Mol Biol       Date:  1996-02       Impact factor: 4.076
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.