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B6db families: 4.1.99.2

4.1.99.2
Activity 4.1.99.2
Description Tyrosine phenol-lyase
Notes A group of closely related bacterial sequences, very similar to tryptophanases (family 4.1.99.1).
PDB 1TPL;2TPL;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Reference sequence TPL_CITFR
Domain interval 46-423
Catalytic site 257 K
 
References
 Zheng RC, Tang XL, Suo H, Feng LL, Liu X, Yang J, Zheng YG (2018) Biochemical characterization of a novel tyrosine phenol-lyase from Fusobacterium nucleatum for highly efficient biosynthesis of l-DOPA Enzyme Microb Technol 112 88-93.

 Lee, S. G.; Hong, S. P.; Choi, Y. H.; Chung, Y. J.; Sung, M. H. (1997) Thermostable tyrosine phenol-lyase of Symbiobacterium sp. SC-1: gene cloning, sequence determination, and overproduction in Escherichia coli Protein Expr Purif 11 263-70.

 Sundararaju, B.; Antson, A. A.; Phillips, R. S.; Demidkina, T. V.; Barbolina, M. V.; Gollnick, P.; Dodson, G. G.; Wilson, K. S. (1997) The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site- directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity Biochemistry 36 6502-10.

 Iwamori, S.; Oikawa, T.; Ishiwata, K.; Makiguchi, N. (1992) Cloning and expression of the Erwinia herbicola tyrosine phenol-lyase gene in Escherichia coli Biotechnol Appl Biochem 16 77-85.

Articles on 4.1.99.2
last changed 2008/01/29 19:54

B6db families