MUTANT ACCESSION NUMBER: 91
PROTEIN NAME: Tyrosine phenol-lyase (EC 4.1.99.2) (Beta-tyrosinase).
SWISS PROT ENTRY:
TPL_CITFR
ORGANISM: CITROBACTER FREUNDII
GENE NAME: TPL
VARIANT OR MUTAGEN:Mutagen
PMD ENTRY: A976853
MUTATIONS:
POINT Arg 381 Ala
EFFECTS: Binding of PLP to the protein [=]: kcat [-] and kcat/Km [-] for L-tyrosine: kcat [-]and kcat/Km [+] for S-alkyl-L-cysteines: Substrate specificity for SOPC, O-benzyl-L-serine, O-benzoyl- L-serine and beta-chloro-L-alanine [=]: Effect of pH on the reaction with L-tyrosine [-]: Ki for L-tryptophan [-] and for L-phenylalanine [+]: Ability to form quinonoid intermediate from L-tyrosine [=] (by rapid-scanning stopped-flow reaction)
REFERENCE:
PUBMED ID:
9174368
TITLE: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.
AUTHOR:Sundararaju B, Antson AA, Phillips RS, Demidkina TV, Barbolina MV, Gollnick P, Dodson GG, Wilson KS.
REFERENCE:Biochemistry. 1997 May 27;36(21):6502-10.
3D STRUCTURE:1TPL 2TPL
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