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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.
Sundararaju B, Antson AA, Phillips RS, Demidkina TV, Barbolina MV, Gollnick P, Dodson GG, Wilson KS. Sundararaju B, et al. Biochemistry. 1997 May 27;36(21):6502-10. doi: 10.1021/bi962917+. Biochemistry. 1997. PMID: 9174368
Role of lysine-256 in Citrobacter freundii tyrosine phenol-lyase in monovalent cation activation.
Phillips RS, Chen HY, Shim D, Lima S, Tavakoli K, Sundararaju B. Phillips RS, et al. Among authors: sundararaju b. Biochemistry. 2004 Nov 16;43(45):14412-9. doi: 10.1021/bi0484062. Biochemistry. 2004. PMID: 15533046
We have shown previously that Glu-69, which is a ligand to the bound cation, is important in monovalent cation binding and activation [Sundararaju, B., Chen, H., Shillcutt, S., and Phillips, R. S. (2000) Biochemistry 39, 8546-8555]. ...
We have shown previously that Glu-69, which is a ligand to the bound cation, is important in monovalent cation binding and activation [Su …
The catalytic mechanism of kynureninase from Pseudomonas fluorescens: evidence for transient quinonoid and ketimine intermediates from rapid-scanning stopped-flow spectrophotometry.
Phillips RS, Sundararaju B, Koushik SV. Phillips RS, et al. Among authors: sundararaju b. Biochemistry. 1998 Jun 16;37(24):8783-9. doi: 10.1021/bi980066v. Biochemistry. 1998. PMID: 9628740
These data demonstrate that quinonoid and ketimine intermediates are catalytically competent in the reaction mechanism of kynureninase, and provide additional support for our proposed mechanism for kynureninase from steady-state kinetic studies [Koushik, S. V., Sundararaju …
These data demonstrate that quinonoid and ketimine intermediates are catalytically competent in the reaction mechanism of kynureninase, and …
55 results