Literature DB >> 2306129

Chlorophyll-free chromoplasts from daffodil contain most of the enzymes for chlorophyll synthesis in a highly active form.

M Lützow1, H Kleinig.   

Abstract

Chromoplasts isolated from chlorophyll-free daffodil flowers utilize in vitro delta-aminolevulinic acid (ALA) as precursor for the synthesis of large amounts of at least nine different products. Their identification as intermediates of the chlorophyll biosynthetic pathway demonstrates the presence of the majority of the respective enzymes in this nongreen plastid preparation. Porphobilinogen synthase was investigated more closely and found to be similar in its properties to the corresponding enzyme from other plastid sources. Protoporphyrin IX was also accepted as a substrate by chromoplast homogenate; here, as in the case of ALA as a substrate, Mg-protoporphyrin IX monomethyl ester was the last product formed. Formation of the isocyclic chlorophyll ring was not observed.

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Year:  1990        PMID: 2306129     DOI: 10.1016/0003-9861(90)90555-d

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  2 in total

1.  Expression and subcellular location of the tetrapyrrole synthesis enzyme porphobilinogen deaminase in light-grown Euglena gracilis and three nonchlorophyllous cell lines.

Authors:  L S Shashidhara; A G Smith
Journal:  Proc Natl Acad Sci U S A       Date:  1991-01-01       Impact factor: 11.205

2.  The wound-inducible Lls1 gene from maize is an orthologue of the Arabidopsis Acd1 gene, and the LLS1 protein is present in non-photosynthetic tissues.

Authors:  Manli Yang; Ellen Wardzala; Gurmukh S Johal; John Gray
Journal:  Plant Mol Biol       Date:  2004-01       Impact factor: 4.076

  2 in total

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