The influence of metal ions on malic enzyme activity and lipid synthesis in Aspergillus niger

被引:39
作者
Jernejc, K [1 ]
Legisa, M [1 ]
机构
[1] Natl Inst Chem, Ljubljana 1001, Slovenia
关键词
malic enzyme; copper ion; metal inhibition; lipids; citric acid;
D O I
10.1111/j.1574-6968.2002.tb11473.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
In the presence of copper significant induction of citric acid overflow was observed, while concomitantly lower levels of total lipids were detected in the cells. Its effect was more obvious in a medium with magnesium as sole divalent metal ions, while in a medium with magnesium and manganese the addition of copper had a less pronounced effect. Since the malic enzyme was recognised as a supplier of reducing power in the form of reduced nicotinamide adenine dinucleotide phosphate for lipid biosynthesis, its kinetic parameters with regard to different concentrations of metal ions were investigated. Some inhibition was found with Fe2+ and Zn2+, while Cu2+ ions in a concentration of 0.1 mM completely abolished malic enzyme activity. The same metal ions proportionally reduced the levels of total lipids in Aspergillus niger cells. A strong competitive inhibition of the enzyme by Cu2+ was observed. It seemed that copper competes with Mg2+ and Mn2+ for the same binding site on the protein. (C) 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:185 / 190
页数:6
相关论文
共 23 条
[1]   ROLE OF METAL COFACTORS IN ENZYME REGULATION - DIFFERENCES IN THE REGULATORY PROPERTIES OF THE ESCHERICHIA-COLI NICOTINAMIDE ADENINE-DINUCLEOTIDE PHOSPHATE SPECIFIC MALIC ENZYME, DEPENDING ON WHETHER MAGNESIUM-ION OR MANGANESE ION SERVES AS DIVALENT-CATION [J].
BROWN, DA ;
COOK, RA .
BIOCHEMISTRY, 1981, 20 (09) :2503-2512
[2]   Involvement of Phe(19) in the Mn2+-L-malate binding and the subunit interactions of pigeon liver malic enzyme [J].
Chou, WY ;
Liu, MY ;
Huang, SM ;
Chang, GG .
BIOCHEMISTRY, 1996, 35 (30) :9873-9879
[3]   SELECTIVE OXIDATIVE MODIFICATION AND AFFINITY CLEAVAGE OF PIGEON LIVER MALIC ENZYME BY THE CU2+-ASCORBATE SYSTEM [J].
CHOU, WY ;
TSAI, WP ;
LIN, CC ;
CHANG, GG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (43) :25935-25941
[4]   EFFECT OF MANGANESE AND OTHER HEAVY METALS ON SUBMERGED CITRIC ACID FERMENTATION OF MOLASSES [J].
CLARK, DS ;
ITO, K ;
HORITSU, H .
BIOTECHNOLOGY AND BIOENGINEERING, 1966, 8 (04) :465-&
[5]  
FOLCH J, 1957, J BIOL CHEM, V226, P497
[6]   Negative fungal chemotropism to toxic metals [J].
Fomina, M ;
Ritz, K ;
Gadd, GM .
FEMS MICROBIOLOGY LETTERS, 2000, 193 (02) :207-211
[7]   ISOTOPE EFFECT STUDIES OF CHICKEN LIVER NADP MALIC ENZYME - ROLE OF THE METAL-ION AND VISCOSITY DEPENDENCE [J].
GRISSOM, CB ;
CLELAND, WW .
BIOCHEMISTRY, 1988, 27 (08) :2927-2934
[8]  
Hsu RY., 1969, Methods in Enzymology, V13, P230, DOI DOI 10.1016/0076-6879(69)13042-6
[9]   Slow binding of metal ions to pigeon liver malic enzyme: A general case [J].
Hung, HC ;
Chang, GG ;
Yang, ZR ;
Tong, L .
BIOCHEMISTRY, 2000, 39 (46) :14095-14102
[10]   CITRIC-ACID PRODUCTION IN CHEMICALLY DEFINED MEDIA BY ASPERGILLUS-NIGER [J].
JERNEJC, K ;
CIMERMAN, A ;
PERDIH, A .
EUROPEAN JOURNAL OF APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 1982, 14 (01) :29-33