Wheat acetyl-CoA carboxylase

The acetyl-CoA carboxylase present in both wheat germ and total wheat leaf protein contains ca. 220 kDa subunits. It is the major biotin-dependent carboxylase present in wheat chloroplasts. Active acetyl-CoA carboxylase purified from wheat germ is a homodimer with an apparent molecular mass of ca. 5...

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Bibliographic Details
Published inPlant molecular biology Vol. 22; no. 3; p. 547
Main Authors Gornicki, P. (Chicago Univ., Chicago, IL (USA). Dept. of Molecular Genetics and Cell Biology), Haselkorn, R
Format Journal Article
LanguageEnglish
Published Netherlands 01.06.1993
Subjects
Acetyl-CoA Carboxylase - chemistry
Acetyl-CoA Carboxylase - drug effects
Acetyl-CoA Carboxylase - isolation & purification
Amino Acid Sequence
CEREAL GERMS
CHLOROPLASTE
CHLOROPLASTS
CLOROPLASTO
FEUILLE
GERME DE CEREALE
GERMENES DE CEREALES
HERBICIDAS
HERBICIDE
HERBICIDES
Herbicides - pharmacology
HOJAS
LEAVES
LIGASAS
LIGASE
LIGASES
Molecular Sequence Data
PROTEINAS
PROTEINE
PROTEINS
Pyridines - pharmacology
TRITICUM
Triticum - enzymology
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Summary:The acetyl-CoA carboxylase present in both wheat germ and total wheat leaf protein contains ca. 220 kDa subunits. It is the major biotin-dependent carboxylase present in wheat chloroplasts. Active acetyl-CoA carboxylase purified from wheat germ is a homodimer with an apparent molecular mass of ca. 500 kDa. The enzyme from wheat germ or from wheat chloroplasts is sensitive to the herbicide haloxyfop at micromolar levels. The incorporation of 14C-acetate into fatty acids in freshly cut wheat seedling leaves provides a convenient in vivo assay for both acetyl-CoA carboxylase and haloxyfop.
Bibliography:9304779
F30
ISSN:0167-4412
1573-5028
DOI:10.1007/bf00015984