Aminolevulinic acid dehydratase in pea (Pisum sativum L.). Identification of an unusual metal-binding domain in the plant enzyme.
Open Access
- 1 September 1991
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (26) , 17060-17066
- https://doi.org/10.1016/s0021-9258(19)47339-0
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- The δ-aminolevulinate dehydratases: Molecular and environmental propertiesPublished by Springer Nature ,2007
- Poly(A) signalsCell, 1991
- Isolation, characterization and partial amino acid sequence of a chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.)Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequencesJournal of Molecular Evolution, 1990
- 5-aminolevulinate dehydratase activity in thylakoid-related structures of etiochloroplasts from radish cotyledonsPhytochemistry, 1988
- Histidine residues at the active site of maize δ-aminolevulinic acid dehydratasePhytochemistry, 1985
- Stimulation par la lumiere rouge lointain de la synthese de la delta-aminolevulinate deshydratase des cotyledons de radisPhysiologia Plantarum, 1984
- Molecular properties of 5‐aminolevulinic acid dehydratase from Spinacia oleraceaEuropean Journal of Biochemistry, 1983
- 5-Aminolaevulinic acid dehydratase: structure, function, and mechanismPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1976
- Quaternary structure of δ-aminolevulinate dehydratase from Rhodopseudomonas spheroidesBiochemistry, 1971