An Auxin Inactivation System Involving Tyrosinase
- 1 March 1956
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 31 (2) , 165-167
- https://doi.org/10.1104/pp.31.2.165
Abstract
Indoleacetic acid (IAA) is inactivated by mushroom tyrosinase or a tyrosinase present in dialyzed extracts of growing leaves of the fern Osmunda cinnamomea, but only in the presence of certain phenols, such as catechol or pyrogallol. Tyrosine and 3,4-dihydroxyphenylalanine do not promote IAA inactivation althpugh these phenols are oxidized by the enzyme. It appears probable that a reaction occurs between IAA and one of the intermediate compounds formed during the oxidation of catechol or pyrogallol. Possible mechanisms for the reaction, as well as its implications for auxin destruction in plant extracts are discussed.Keywords
This publication has 8 references indexed in Scilit:
- Enzymatic Auxin Inactivation by Extracts of the Fern, Osmunda cinnamomea L.Plant Physiology, 1955
- The Role of 2,4-Dichlorophenol in the Destruction of Indoleacetic Acid by Peroxidase.Plant Physiology, 1955
- The oxidation of indolyl-3-acetic acid by waxpod bean root sap and peroxidase systemsBiochemical Journal, 1955
- Flavoprotein and peroxidase as components of the indoleacetic acid oxidase system of peasArchives of Biochemistry and Biophysics, 1953
- Hydrogen Peroxide in the Enzymic Oxidation of HeteroauxinAustralian Journal of Biological Sciences, 1951
- INDOLEACETIC ACID INACTIVATING ENZYMES FROM BEAN ROOTS AND PEA SEEDLINGS1950
- THE CHEMISTRY OF MELANIN .6. MECHANISM OF THE OXIDATION OF CATECHOL BY TYROSINASE1949
- On the Nature of the Enzyme TyrosinaseJournal of the American Chemical Society, 1938