LIPOXYGENASE OF THE THERMOPHILIC BACTERIA THERMOACTINOMYCES-VULGARIS - PROPERTIES AND STUDY ON THE ACTIVE-SITE

被引：18

作者：

INY, D ^{[1
]}

GROSSMAN, S ^{[1
]}

PINSKY, A ^{[1
]}

机构：

[1] BAR ILAN UNIV,DEPT LIFE SCI,IL-52900 RAMAT GAN,ISRAEL

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1993年 / 25卷 / 09期

关键词：

D O I：

10.1016/0020-711X(93)90085-S

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. A lipoxygenase activity was purified from Thermoactinomyces vulgaris and some of its properties were characterized. 2. The enzyme showed a temperature activity range of 40-55-degrees-C with still significant activity over 60-degrees-C. 3. The pH of activity on linoleic acid had a broad range with an optimum at pH 6.0 and a weaker one at pH 11.0. 4. On arachidonic acid the pattern was narrow bell-shaped with an optimum at pH 6.5, 5. The purified lipoxygenase from Th. vulgaris showed an apparent K(m) of 1 mM and V(max) of 0.84 mumol diene/min/mg protein. 6. It was inhibited by the oxidation products, 9-HPOD and 13-HPOD. 7. A 160,000 Da molecular weight of the enzyme was determined by molecular filtration. Methionine, tyrosine, tryptophan and cysteine are apparently involved in its activity.

引用

页码：1325 / 1330

页数：6

共 35 条

[1] LINOLEATE OXIDATION INDUCED BY LIPOXYGENASE AND HEME PROTEINS - A DIRECT SPECTROPHOTOMETRIC ASSAY [J].