从以邻苯二甲酸盐培养的赭黄假单胞菌中纯化γ-草酰苹果酸水合酶及其性质

Purification and properties of gamma-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate.

作者信息

Maruyama K

出版信息

Biochem Biophys Res Commun. 1985 Apr 16;128(1):271-7. doi: 10.1016/0006-291x(85)91674-2.

DOI:10.1016/0006-291x(85)91674-2

Abstract

Pseudomonas ochraceae produced inducibly a hydro-lyase which catalyzes the reversible conversion of gamma-oxalomesaconate into (-)-gamma-oxalocitramalate. The enzyme has been purified to homogeneity from the bacteria grown with phthalate. The enzyme was a dimeric protein (pI=4.9) with a Mr of 68,000 and showed a high specificity for gamma-oxalomesaconate (Km=14 microM) and (-)-gamma-oxalocitramalate (Km=6.4 microM). Equilibrium constant for the hydration of gamma-oxalomesaconate at pH 8.0 and 24 degrees C was 2.5. Various thiols activated the enzyme.

摘要

赭黄假单胞菌可诱导产生一种水解酶，该酶催化γ-草酰苹果酸可逆转化为(-)-γ-草酰柠苹酸。已从在邻苯二甲酸盐存在下生长的细菌中纯化得到了均一的该酶。该酶是一种二聚体蛋白（pI = 4.9），Mr为68,000，对γ-草酰苹果酸（Km = 14 μM）和(-)-γ-草酰柠苹酸（Km = 6.4 μM）表现出高特异性。在pH 8.0和24℃条件下，γ-草酰苹果酸水合作用的平衡常数为2.5。各种硫醇可激活该酶。

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