Aminolevulinic acid dehydratase in pea (Pisum sativum L.): Identification of an unusual metal-binding domain in the plant enzyme

Keyphrases

• Pisum Sativum 100%
• Plant Enzymes 100%
• Metal-binding Domain 100%
• δ-Aminolevulinic Acid Dehydratase 100%
• ALA Dehydratase 66%
• Complementary DNA (cDNA) 33%
• Lysine 16%
• Catalytic Activity 16%
• Higher Plants 16%
• Chlorophyll a (Chl a) 16%
• Mg2+ 16%
• Active Sites 16%
• Domain-independent 16%
• Steady State 16%
• Plant Cells 16%
• Heme 16%
• Amino Acid Sequence 16%
• Northern Blot Analysis 16%
• Aspartate 16%
• Light-induced 16%
• Ligand-binding Domain 16%
• Tetrapyrrole 16%
• Poly(A)+ RNA 16%
• Spinach Leaves 16%
• Zn2+-binding 16%
• Metal-ligand Binding 16%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Metal Binding 100%
• Binding Domain 100%
• Pisum 100%
• Porphobilinogen Synthase 100%
• Dehydratase 66%
• Alpha-Linolenic Acid 66%
• Messenger RNA 33%
• Lysine 16%
• Peptide Sequence 16%
• RNA 16%
• Steady State 16%
• Active Site 16%
• Enzymatic Activity 16%
• Aspartic Acid 16%
• Chlorophyll 16%
• Northern Blotting 16%
• Ligand Binding Domain 16%

Agricultural and Biological Sciences

• Pea 100%
• Porphobilinogen Synthase 100%
• Alpha-Linolenic Acid 50%
• Messenger RNA 25%
• Chlorophyll 12%
• Aspartic Acid 12%
• Amino Acid Sequence 12%
• Heme 12%
• cDNA Libraries 12%
• Lysine 12%
• Northern Blotting 12%