[中间柠檬酸杆菌酪氨酸酚裂解酶的分离与性质]

[Isolation and properties of tyrosine phenol-lyase from Citrobacter intermedius].

作者信息

Demidkina T V, Miagkikh I V, Faleev N G, Belikov V M

出版信息

Biokhimiia. 1984 Jan;49(1):32-7.

Abstract

A method for preparation of homogeneous tyrosine phenol lyase (EC 4.199.2) from Citrobacter intermedius has been developed. The cells were cultivated in the media with a view to obtain a cell culture with a high activity of tyrosine phenol lyase. The isoelectric point for the enzyme lies at pH 4.9. Tyrosine phenol lyase is strictly stereospecific: it catalyzes the formation of pyruvate only from L-tyrosine, but not from D-tyrosine. Kinetic studies showed that K+ and NH4+ cations are non-competitive activators of the enzyme (Ka = 3.57 X 10(-3) and 1.34 X 10(-4) M, respectively).

摘要

已开发出一种从中间柠檬酸杆菌制备均一酪氨酸酚裂解酶（EC 4.199.2）的方法。培养细胞所用的培养基旨在获得具有高酪氨酸酚裂解酶活性的细胞培养物。该酶的等电点为pH 4.9。酪氨酸酚裂解酶具有严格的立体特异性：它仅催化由L - 酪氨酸形成丙酮酸，而不催化由D - 酪氨酸形成丙酮酸。动力学研究表明，K⁺和NH₄⁺阳离子是该酶的非竞争性激活剂（Ka分别为3.57×10⁻³和1.34×10⁻⁴ M）。