2004
DOI: 10.1021/bi0484062
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Role of Lysine-256 in Citrobacter freundii Tyrosine Phenol-lyase in Monovalent Cation Activation

Abstract: Tyrosine phenol-lyase (TPL) from Citrobacter freundii is dependent on monovalent cations, K(+) or NH(4)(+), for high activity. 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]. Lys-256 is located in the monovalent cation binding site of TPL, where it forms a hydrogen bond with a structural water bound to the cation. This lysine re… Show more

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Cited by 7 publications
(4 citation statements)
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References 38 publications
(56 reference statements)
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“…This water molecule lies in the active site, and it is hydrogen-bonded by the PLP phosphate group and hydroxyl groups from side chains of the active site residues Ser51, Tyr71, and Tyr291 (Figure 3). These concatenated interactions of the cation-binding site with the active site residues demonstrate the critical role of Lys256 in the formation of the monovalent cation binding site in agreement with previous biochemical observations (47) and provide an insight into the influence of monovalent cations on the activity of TPL (48,49). At cation concentrations lower than 100 mM, K + , NH 4 + , and Rb + were shown to be the most effective activators, Cs + and Li + were significantly less effective, while the effect of Na + was negligible.…”
Section: Resultssupporting
confidence: 91%
“…This water molecule lies in the active site, and it is hydrogen-bonded by the PLP phosphate group and hydroxyl groups from side chains of the active site residues Ser51, Tyr71, and Tyr291 (Figure 3). These concatenated interactions of the cation-binding site with the active site residues demonstrate the critical role of Lys256 in the formation of the monovalent cation binding site in agreement with previous biochemical observations (47) and provide an insight into the influence of monovalent cations on the activity of TPL (48,49). At cation concentrations lower than 100 mM, K + , NH 4 + , and Rb + were shown to be the most effective activators, Cs + and Li + were significantly less effective, while the effect of Na + was negligible.…”
Section: Resultssupporting
confidence: 91%
“…A unique feature of TIL and TPL is another strictly conserved lysine (Lys-256 in C. freundii TPL) immediately preceding the PLP-binding lysine, and hydrogen bonded to a water molecule bound to the MVC. This lysine appears to play a role in the activation of these enzymes by MVCs [24]. The residues that contact the substrate directly include a conserved tyrosine (Tyr- (Fig.…”
Section: Structure Of Til and Tplmentioning
confidence: 99%
“…The network of hydrogen bonds and salt bridges formed upon the binding of PLP is known to influence the quaternary structure of tryptophanases [17]. Therefore, when considering the common structural features of α‐family PLP enzymes [26,27], the T15A mutation on the N‐terminal arm may have increased the rigidity of the cofactor binding architecture of C. freundii TPL through adjusting the quaternary interfaces. One possible communication between the N‐terminal arm and the active site is through Tyr71, which belongs to the adjacent subunit of the catalytic dimer.…”
Section: Discussionmentioning
confidence: 99%