Isolation and Purification of Tyrosine Hydroxylase from Callus Cultures of Portulaca grandiflora
Open Access
- 15 September 2001
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 42 (9) , 969-975
- https://doi.org/10.1093/pcp/pce125
Abstract
Tyrosine hydroxylase was separated from polyphenol oxidase activity and was highly purified from betacyanin producing callus cultures of Portulaca grandiflora. The purified enzyme catalyzed the formation of DOPA (l-3,4-dihydroxyphenylalanine) from tyrosine and required the pterin compounds (6-methyl-5,6,7,8-tetrahydropterin; 5,6,7,8-tetrahydrobiopterin; 6,7-dimethyl-5,6,7,8-tetrahydropterin) as coenzyme. The Km values for tyrosine and 6-methyl-5,6,7,8-tetrahydropterin were 0.5 mM and 0.15 mM, respectively. This enzyme was activated by Fe2+ and Mn2+, and inhibited by metal chelating agents.Keywords
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