| EC |
1.11.2.6 |
| Accepted name: |
L-tyrosine peroxygenase |
| Reaction: |
L-tyrosine + H2O2 = L-dopa + H2O |
| Systematic name: |
L-tyrosine:hydrogen-peroxide oxidoreductase (L-dopa-forming) |
| Comments: |
The enzyme from the bacterium Streptomyces lincolnensis participates in the biosynthesis of the antibiotic lincomycin A, while that from Streptomyces refuineus is involved in anthramycin biosynthesis. The enzyme, which contains a heme b cofactor, is rapidly inactivated in the presence of hydrogen peroxide, but the presence of L-tyrosine protects it. cf. EC 1.11.2.5, 3-methyl-L-tyrosine peroxygenase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Neusser, D., Schmidt, H., Spizek, J., Novotna, J., Peschke, U., Kaschabeck, S., Tichy, P. and Piepersberg, W. The genes lmbB1 and lmbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of L-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A. Arch. Microbiol. 169 (1998) 322–332. [PMID: 9531633] |
| 2. |
Connor, K.L., Colabroy, K.L. and Gerratana, B. A heme peroxidase with a functional role as an L-tyrosine hydroxylase in the biosynthesis of anthramycin. Biochemistry 50 (2011) 8926–8936. [PMID: 21919439] |
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| [EC 1.11.2.6 created 2020] |
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